Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances

Abstract Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of β-amyloid peptides (1–11), (33–42), (1–42) and non-β-amyloid component of Alzheimer’s disease peptide yielded interpretable spectra for all of the peptides pres...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Trimpin, Sarah [verfasserIn] Deinzer, Max L.

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2007

Schlagwörter:	Amyloid Peptide MALDI Plate MALDI Analysis Soluble Peptide Hydrophilic Peptide

Anmerkung:	© American Society for Mass Spectrometry 2007

Übergeordnetes Werk:	Enthalten in: Journal of the American Society for Mass Spectrometry - Washington, DC : ACS Publications, 1990, 18(2007), 8 vom: 01. Aug., Seite 1533-1543
Übergeordnetes Werk:	volume:18 ; year:2007 ; number:8 ; day:01 ; month:08 ; pages:1533-1543

Links:	Volltext

DOI / URN:	10.1016/j.jasms.2007.04.017

Katalog-ID:	SPR031495427

Internformat


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100	1		\|a Trimpin, Sarah \|e verfasserin \|4 aut
245	1	0	\|a Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances
264		1	\|c 2007
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520			\|a Abstract Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of β-amyloid peptides (1–11), (33–42), (1–42) and non-β-amyloid component of Alzheimer’s disease peptide yielded interpretable spectra for all of the peptides present regardless of their relative amounts in the samples. This was not the case for solvent-based MALDI analysis using traditional acidic aqueous/organic solvent conditions, which resulted in severe over-representation of hydrophilic peptide (1–11) and provided no spectra for insoluble amphiphilic peptide (1–42) even when present at 50% relative molar amount. Less accurate representation of components in mixtures by the traditional method appears to be a combination of poor dissolution of peptides in the solvent and preferential ionization of more hydrophilic peptides in the mixture. Consequently, only MBM provided a complete tryptic map of β-amyloid (1–42) compared to 67% coverage by traditional MALDI. Acetonitrile (0.1% TFA) led to improved coverage only at a 50% molar ratio of peptide (1–42), but also to a side product of (1–42), Met oxidation (amino acid 35), a phenomenon not observed in MBM MALDI analysis. Traditional MALDI analysis resulted in over-representation of hydrophilic soluble β-amyloid (1–11) in defined mixtures and autoproteolytic peptides of trypsin. In contrast, over-representation and under-representation were less pronounced in solvent-free MALDI in all of the investigated cases. Analysis of defined peptide and tryptic peptide mixtures showed that MBM MALDI yielded greater qualitative reliability, which also improved quantitative response relative to the solvent-based approach.
650		4	\|a Amyloid Peptide \|7 (dpeaa)DE-He213
650		4	\|a MALDI Plate \|7 (dpeaa)DE-He213
650		4	\|a MALDI Analysis \|7 (dpeaa)DE-He213
650		4	\|a Soluble Peptide \|7 (dpeaa)DE-He213
650		4	\|a Hydrophilic Peptide \|7 (dpeaa)DE-He213
700	1		\|a Deinzer, Max L. \|4 aut
773	0	8	\|i Enthalten in \|t Journal of the American Society for Mass Spectrometry \|d Washington, DC : ACS Publications, 1990 \|g 18(2007), 8 vom: 01. Aug., Seite 1533-1543 \|w (DE-627)320598799 \|w (DE-600)2019911-9 \|x 1879-1123 \|7 nnns
773	1	8	\|g volume:18 \|g year:2007 \|g number:8 \|g day:01 \|g month:08 \|g pages:1533-1543
856	4	0	\|u https://dx.doi.org/10.1016/j.jasms.2007.04.017 \|z lizenzpflichtig \|3 Volltext
912			\|a GBV_USEFLAG_A
912			\|a SYSFLAG_A
912			\|a GBV_SPRINGER
912			\|a SSG-OLC-PHA
912			\|a GBV_ILN_20
912			\|a GBV_ILN_22
912			\|a GBV_ILN_23
912			\|a GBV_ILN_24
912			\|a GBV_ILN_31
912			\|a GBV_ILN_32
912			\|a GBV_ILN_39
912			\|a GBV_ILN_40
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_74
912			\|a GBV_ILN_95
912			\|a GBV_ILN_100
912			\|a GBV_ILN_101
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_120
912			\|a GBV_ILN_138
912			\|a GBV_ILN_150
912			\|a GBV_ILN_151
912			\|a GBV_ILN_152
912			\|a GBV_ILN_161
912			\|a GBV_ILN_170
912			\|a GBV_ILN_187
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_647
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2031
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2037
912			\|a GBV_ILN_2038
912			\|a GBV_ILN_2039
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2070
912			\|a GBV_ILN_2086
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2108
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2116
912			\|a GBV_ILN_2118
912			\|a GBV_ILN_2119
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2144
912			\|a GBV_ILN_2147
912			\|a GBV_ILN_2148
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2188
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_2522
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4046
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4246
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4328
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4335
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4367
912			\|a GBV_ILN_4393
912			\|a GBV_ILN_4700
951			\|a AR
952			\|d 18 \|j 2007 \|e 8 \|b 01 \|c 08 \|h 1533-1543

Indexfelder

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publishDate	2007
allfields	10.1016/j.jasms.2007.04.017 doi (DE-627)SPR031495427 (SPR)j.jasms.2007.04.017-e DE-627 ger DE-627 rakwb eng Trimpin, Sarah verfasserin aut Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © American Society for Mass Spectrometry 2007 Abstract Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of β-amyloid peptides (1–11), (33–42), (1–42) and non-β-amyloid component of Alzheimer’s disease peptide yielded interpretable spectra for all of the peptides present regardless of their relative amounts in the samples. This was not the case for solvent-based MALDI analysis using traditional acidic aqueous/organic solvent conditions, which resulted in severe over-representation of hydrophilic peptide (1–11) and provided no spectra for insoluble amphiphilic peptide (1–42) even when present at 50% relative molar amount. Less accurate representation of components in mixtures by the traditional method appears to be a combination of poor dissolution of peptides in the solvent and preferential ionization of more hydrophilic peptides in the mixture. Consequently, only MBM provided a complete tryptic map of β-amyloid (1–42) compared to 67% coverage by traditional MALDI. Acetonitrile (0.1% TFA) led to improved coverage only at a 50% molar ratio of peptide (1–42), but also to a side product of (1–42), Met oxidation (amino acid 35), a phenomenon not observed in MBM MALDI analysis. Traditional MALDI analysis resulted in over-representation of hydrophilic soluble β-amyloid (1–11) in defined mixtures and autoproteolytic peptides of trypsin. In contrast, over-representation and under-representation were less pronounced in solvent-free MALDI in all of the investigated cases. Analysis of defined peptide and tryptic peptide mixtures showed that MBM MALDI yielded greater qualitative reliability, which also improved quantitative response relative to the solvent-based approach. Amyloid Peptide (dpeaa)DE-He213 MALDI Plate (dpeaa)DE-He213 MALDI Analysis (dpeaa)DE-He213 Soluble Peptide (dpeaa)DE-He213 Hydrophilic Peptide (dpeaa)DE-He213 Deinzer, Max L. aut Enthalten in Journal of the American Society for Mass Spectrometry Washington, DC : ACS Publications, 1990 18(2007), 8 vom: 01. Aug., Seite 1533-1543 (DE-627)320598799 (DE-600)2019911-9 1879-1123 nnns volume:18 year:2007 number:8 day:01 month:08 pages:1533-1543 https://dx.doi.org/10.1016/j.jasms.2007.04.017 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 2007 8 01 08 1533-1543
spelling	10.1016/j.jasms.2007.04.017 doi (DE-627)SPR031495427 (SPR)j.jasms.2007.04.017-e DE-627 ger DE-627 rakwb eng Trimpin, Sarah verfasserin aut Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © American Society for Mass Spectrometry 2007 Abstract Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of β-amyloid peptides (1–11), (33–42), (1–42) and non-β-amyloid component of Alzheimer’s disease peptide yielded interpretable spectra for all of the peptides present regardless of their relative amounts in the samples. This was not the case for solvent-based MALDI analysis using traditional acidic aqueous/organic solvent conditions, which resulted in severe over-representation of hydrophilic peptide (1–11) and provided no spectra for insoluble amphiphilic peptide (1–42) even when present at 50% relative molar amount. Less accurate representation of components in mixtures by the traditional method appears to be a combination of poor dissolution of peptides in the solvent and preferential ionization of more hydrophilic peptides in the mixture. Consequently, only MBM provided a complete tryptic map of β-amyloid (1–42) compared to 67% coverage by traditional MALDI. Acetonitrile (0.1% TFA) led to improved coverage only at a 50% molar ratio of peptide (1–42), but also to a side product of (1–42), Met oxidation (amino acid 35), a phenomenon not observed in MBM MALDI analysis. Traditional MALDI analysis resulted in over-representation of hydrophilic soluble β-amyloid (1–11) in defined mixtures and autoproteolytic peptides of trypsin. In contrast, over-representation and under-representation were less pronounced in solvent-free MALDI in all of the investigated cases. Analysis of defined peptide and tryptic peptide mixtures showed that MBM MALDI yielded greater qualitative reliability, which also improved quantitative response relative to the solvent-based approach. Amyloid Peptide (dpeaa)DE-He213 MALDI Plate (dpeaa)DE-He213 MALDI Analysis (dpeaa)DE-He213 Soluble Peptide (dpeaa)DE-He213 Hydrophilic Peptide (dpeaa)DE-He213 Deinzer, Max L. aut Enthalten in Journal of the American Society for Mass Spectrometry Washington, DC : ACS Publications, 1990 18(2007), 8 vom: 01. Aug., Seite 1533-1543 (DE-627)320598799 (DE-600)2019911-9 1879-1123 nnns volume:18 year:2007 number:8 day:01 month:08 pages:1533-1543 https://dx.doi.org/10.1016/j.jasms.2007.04.017 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 2007 8 01 08 1533-1543
allfields_unstemmed	10.1016/j.jasms.2007.04.017 doi (DE-627)SPR031495427 (SPR)j.jasms.2007.04.017-e DE-627 ger DE-627 rakwb eng Trimpin, Sarah verfasserin aut Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © American Society for Mass Spectrometry 2007 Abstract Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of β-amyloid peptides (1–11), (33–42), (1–42) and non-β-amyloid component of Alzheimer’s disease peptide yielded interpretable spectra for all of the peptides present regardless of their relative amounts in the samples. This was not the case for solvent-based MALDI analysis using traditional acidic aqueous/organic solvent conditions, which resulted in severe over-representation of hydrophilic peptide (1–11) and provided no spectra for insoluble amphiphilic peptide (1–42) even when present at 50% relative molar amount. Less accurate representation of components in mixtures by the traditional method appears to be a combination of poor dissolution of peptides in the solvent and preferential ionization of more hydrophilic peptides in the mixture. Consequently, only MBM provided a complete tryptic map of β-amyloid (1–42) compared to 67% coverage by traditional MALDI. Acetonitrile (0.1% TFA) led to improved coverage only at a 50% molar ratio of peptide (1–42), but also to a side product of (1–42), Met oxidation (amino acid 35), a phenomenon not observed in MBM MALDI analysis. Traditional MALDI analysis resulted in over-representation of hydrophilic soluble β-amyloid (1–11) in defined mixtures and autoproteolytic peptides of trypsin. In contrast, over-representation and under-representation were less pronounced in solvent-free MALDI in all of the investigated cases. Analysis of defined peptide and tryptic peptide mixtures showed that MBM MALDI yielded greater qualitative reliability, which also improved quantitative response relative to the solvent-based approach. Amyloid Peptide (dpeaa)DE-He213 MALDI Plate (dpeaa)DE-He213 MALDI Analysis (dpeaa)DE-He213 Soluble Peptide (dpeaa)DE-He213 Hydrophilic Peptide (dpeaa)DE-He213 Deinzer, Max L. aut Enthalten in Journal of the American Society for Mass Spectrometry Washington, DC : ACS Publications, 1990 18(2007), 8 vom: 01. Aug., Seite 1533-1543 (DE-627)320598799 (DE-600)2019911-9 1879-1123 nnns volume:18 year:2007 number:8 day:01 month:08 pages:1533-1543 https://dx.doi.org/10.1016/j.jasms.2007.04.017 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 2007 8 01 08 1533-1543
allfieldsGer	10.1016/j.jasms.2007.04.017 doi (DE-627)SPR031495427 (SPR)j.jasms.2007.04.017-e DE-627 ger DE-627 rakwb eng Trimpin, Sarah verfasserin aut Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © American Society for Mass Spectrometry 2007 Abstract Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of β-amyloid peptides (1–11), (33–42), (1–42) and non-β-amyloid component of Alzheimer’s disease peptide yielded interpretable spectra for all of the peptides present regardless of their relative amounts in the samples. This was not the case for solvent-based MALDI analysis using traditional acidic aqueous/organic solvent conditions, which resulted in severe over-representation of hydrophilic peptide (1–11) and provided no spectra for insoluble amphiphilic peptide (1–42) even when present at 50% relative molar amount. Less accurate representation of components in mixtures by the traditional method appears to be a combination of poor dissolution of peptides in the solvent and preferential ionization of more hydrophilic peptides in the mixture. Consequently, only MBM provided a complete tryptic map of β-amyloid (1–42) compared to 67% coverage by traditional MALDI. Acetonitrile (0.1% TFA) led to improved coverage only at a 50% molar ratio of peptide (1–42), but also to a side product of (1–42), Met oxidation (amino acid 35), a phenomenon not observed in MBM MALDI analysis. Traditional MALDI analysis resulted in over-representation of hydrophilic soluble β-amyloid (1–11) in defined mixtures and autoproteolytic peptides of trypsin. In contrast, over-representation and under-representation were less pronounced in solvent-free MALDI in all of the investigated cases. Analysis of defined peptide and tryptic peptide mixtures showed that MBM MALDI yielded greater qualitative reliability, which also improved quantitative response relative to the solvent-based approach. Amyloid Peptide (dpeaa)DE-He213 MALDI Plate (dpeaa)DE-He213 MALDI Analysis (dpeaa)DE-He213 Soluble Peptide (dpeaa)DE-He213 Hydrophilic Peptide (dpeaa)DE-He213 Deinzer, Max L. aut Enthalten in Journal of the American Society for Mass Spectrometry Washington, DC : ACS Publications, 1990 18(2007), 8 vom: 01. Aug., Seite 1533-1543 (DE-627)320598799 (DE-600)2019911-9 1879-1123 nnns volume:18 year:2007 number:8 day:01 month:08 pages:1533-1543 https://dx.doi.org/10.1016/j.jasms.2007.04.017 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 2007 8 01 08 1533-1543
allfieldsSound	10.1016/j.jasms.2007.04.017 doi (DE-627)SPR031495427 (SPR)j.jasms.2007.04.017-e DE-627 ger DE-627 rakwb eng Trimpin, Sarah verfasserin aut Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © American Society for Mass Spectrometry 2007 Abstract Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of β-amyloid peptides (1–11), (33–42), (1–42) and non-β-amyloid component of Alzheimer’s disease peptide yielded interpretable spectra for all of the peptides present regardless of their relative amounts in the samples. This was not the case for solvent-based MALDI analysis using traditional acidic aqueous/organic solvent conditions, which resulted in severe over-representation of hydrophilic peptide (1–11) and provided no spectra for insoluble amphiphilic peptide (1–42) even when present at 50% relative molar amount. Less accurate representation of components in mixtures by the traditional method appears to be a combination of poor dissolution of peptides in the solvent and preferential ionization of more hydrophilic peptides in the mixture. Consequently, only MBM provided a complete tryptic map of β-amyloid (1–42) compared to 67% coverage by traditional MALDI. Acetonitrile (0.1% TFA) led to improved coverage only at a 50% molar ratio of peptide (1–42), but also to a side product of (1–42), Met oxidation (amino acid 35), a phenomenon not observed in MBM MALDI analysis. Traditional MALDI analysis resulted in over-representation of hydrophilic soluble β-amyloid (1–11) in defined mixtures and autoproteolytic peptides of trypsin. In contrast, over-representation and under-representation were less pronounced in solvent-free MALDI in all of the investigated cases. Analysis of defined peptide and tryptic peptide mixtures showed that MBM MALDI yielded greater qualitative reliability, which also improved quantitative response relative to the solvent-based approach. Amyloid Peptide (dpeaa)DE-He213 MALDI Plate (dpeaa)DE-He213 MALDI Analysis (dpeaa)DE-He213 Soluble Peptide (dpeaa)DE-He213 Hydrophilic Peptide (dpeaa)DE-He213 Deinzer, Max L. aut Enthalten in Journal of the American Society for Mass Spectrometry Washington, DC : ACS Publications, 1990 18(2007), 8 vom: 01. Aug., Seite 1533-1543 (DE-627)320598799 (DE-600)2019911-9 1879-1123 nnns volume:18 year:2007 number:8 day:01 month:08 pages:1533-1543 https://dx.doi.org/10.1016/j.jasms.2007.04.017 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 2007 8 01 08 1533-1543
language	English
source	Enthalten in Journal of the American Society for Mass Spectrometry 18(2007), 8 vom: 01. Aug., Seite 1533-1543 volume:18 year:2007 number:8 day:01 month:08 pages:1533-1543
sourceStr	Enthalten in Journal of the American Society for Mass Spectrometry 18(2007), 8 vom: 01. Aug., Seite 1533-1543 volume:18 year:2007 number:8 day:01 month:08 pages:1533-1543
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Amyloid Peptide MALDI Plate MALDI Analysis Soluble Peptide Hydrophilic Peptide
isfreeaccess_bool	false
container_title	Journal of the American Society for Mass Spectrometry
authorswithroles_txt_mv	Trimpin, Sarah @@aut@@ Deinzer, Max L. @@aut@@
publishDateDaySort_date	2007-08-01T00:00:00Z
hierarchy_top_id	320598799
id	SPR031495427
language_de	englisch
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author	Trimpin, Sarah
spellingShingle	Trimpin, Sarah misc Amyloid Peptide misc MALDI Plate misc MALDI Analysis misc Soluble Peptide misc Hydrophilic Peptide Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances
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topic_title	Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances Amyloid Peptide (dpeaa)DE-He213 MALDI Plate (dpeaa)DE-He213 MALDI Analysis (dpeaa)DE-He213 Soluble Peptide (dpeaa)DE-He213 Hydrophilic Peptide (dpeaa)DE-He213
topic	misc Amyloid Peptide misc MALDI Plate misc MALDI Analysis misc Soluble Peptide misc Hydrophilic Peptide
topic_unstemmed	misc Amyloid Peptide misc MALDI Plate misc MALDI Analysis misc Soluble Peptide misc Hydrophilic Peptide
topic_browse	misc Amyloid Peptide misc MALDI Plate misc MALDI Analysis misc Soluble Peptide misc Hydrophilic Peptide
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title	Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances
ctrlnum	(DE-627)SPR031495427 (SPR)j.jasms.2007.04.017-e
title_full	Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances
author_sort	Trimpin, Sarah
journal	Journal of the American Society for Mass Spectrometry
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author_browse	Trimpin, Sarah Deinzer, Max L.
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author-letter	Trimpin, Sarah
doi_str_mv	10.1016/j.jasms.2007.04.017
title_sort	solvent-free maldi-ms for the analysis of β-amyloid peptides via the mini-ball mill approach: qualitative and quantitative advances
title_auth	Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances
abstract	Abstract Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of β-amyloid peptides (1–11), (33–42), (1–42) and non-β-amyloid component of Alzheimer’s disease peptide yielded interpretable spectra for all of the peptides present regardless of their relative amounts in the samples. This was not the case for solvent-based MALDI analysis using traditional acidic aqueous/organic solvent conditions, which resulted in severe over-representation of hydrophilic peptide (1–11) and provided no spectra for insoluble amphiphilic peptide (1–42) even when present at 50% relative molar amount. Less accurate representation of components in mixtures by the traditional method appears to be a combination of poor dissolution of peptides in the solvent and preferential ionization of more hydrophilic peptides in the mixture. Consequently, only MBM provided a complete tryptic map of β-amyloid (1–42) compared to 67% coverage by traditional MALDI. Acetonitrile (0.1% TFA) led to improved coverage only at a 50% molar ratio of peptide (1–42), but also to a side product of (1–42), Met oxidation (amino acid 35), a phenomenon not observed in MBM MALDI analysis. Traditional MALDI analysis resulted in over-representation of hydrophilic soluble β-amyloid (1–11) in defined mixtures and autoproteolytic peptides of trypsin. In contrast, over-representation and under-representation were less pronounced in solvent-free MALDI in all of the investigated cases. Analysis of defined peptide and tryptic peptide mixtures showed that MBM MALDI yielded greater qualitative reliability, which also improved quantitative response relative to the solvent-based approach. © American Society for Mass Spectrometry 2007
abstractGer	Abstract Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of β-amyloid peptides (1–11), (33–42), (1–42) and non-β-amyloid component of Alzheimer’s disease peptide yielded interpretable spectra for all of the peptides present regardless of their relative amounts in the samples. This was not the case for solvent-based MALDI analysis using traditional acidic aqueous/organic solvent conditions, which resulted in severe over-representation of hydrophilic peptide (1–11) and provided no spectra for insoluble amphiphilic peptide (1–42) even when present at 50% relative molar amount. Less accurate representation of components in mixtures by the traditional method appears to be a combination of poor dissolution of peptides in the solvent and preferential ionization of more hydrophilic peptides in the mixture. Consequently, only MBM provided a complete tryptic map of β-amyloid (1–42) compared to 67% coverage by traditional MALDI. Acetonitrile (0.1% TFA) led to improved coverage only at a 50% molar ratio of peptide (1–42), but also to a side product of (1–42), Met oxidation (amino acid 35), a phenomenon not observed in MBM MALDI analysis. Traditional MALDI analysis resulted in over-representation of hydrophilic soluble β-amyloid (1–11) in defined mixtures and autoproteolytic peptides of trypsin. In contrast, over-representation and under-representation were less pronounced in solvent-free MALDI in all of the investigated cases. Analysis of defined peptide and tryptic peptide mixtures showed that MBM MALDI yielded greater qualitative reliability, which also improved quantitative response relative to the solvent-based approach. © American Society for Mass Spectrometry 2007
abstract_unstemmed	Abstract Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of β-amyloid peptides (1–11), (33–42), (1–42) and non-β-amyloid component of Alzheimer’s disease peptide yielded interpretable spectra for all of the peptides present regardless of their relative amounts in the samples. This was not the case for solvent-based MALDI analysis using traditional acidic aqueous/organic solvent conditions, which resulted in severe over-representation of hydrophilic peptide (1–11) and provided no spectra for insoluble amphiphilic peptide (1–42) even when present at 50% relative molar amount. Less accurate representation of components in mixtures by the traditional method appears to be a combination of poor dissolution of peptides in the solvent and preferential ionization of more hydrophilic peptides in the mixture. Consequently, only MBM provided a complete tryptic map of β-amyloid (1–42) compared to 67% coverage by traditional MALDI. Acetonitrile (0.1% TFA) led to improved coverage only at a 50% molar ratio of peptide (1–42), but also to a side product of (1–42), Met oxidation (amino acid 35), a phenomenon not observed in MBM MALDI analysis. Traditional MALDI analysis resulted in over-representation of hydrophilic soluble β-amyloid (1–11) in defined mixtures and autoproteolytic peptides of trypsin. In contrast, over-representation and under-representation were less pronounced in solvent-free MALDI in all of the investigated cases. Analysis of defined peptide and tryptic peptide mixtures showed that MBM MALDI yielded greater qualitative reliability, which also improved quantitative response relative to the solvent-based approach. © American Society for Mass Spectrometry 2007
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title_short	Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances
url	https://dx.doi.org/10.1016/j.jasms.2007.04.017
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doi_str	10.1016/j.jasms.2007.04.017
up_date	2024-07-03T23:59:35.586Z
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fullrecord_marcxml	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR031495427</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230519170708.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201007s2007 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.jasms.2007.04.017</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR031495427</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)j.jasms.2007.04.017-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Trimpin, Sarah</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2007</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© American Society for Mass Spectrometry 2007</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of β-amyloid peptides (1–11), (33–42), (1–42) and non-β-amyloid component of Alzheimer’s disease peptide yielded interpretable spectra for all of the peptides present regardless of their relative amounts in the samples. This was not the case for solvent-based MALDI analysis using traditional acidic aqueous/organic solvent conditions, which resulted in severe over-representation of hydrophilic peptide (1–11) and provided no spectra for insoluble amphiphilic peptide (1–42) even when present at 50% relative molar amount. Less accurate representation of components in mixtures by the traditional method appears to be a combination of poor dissolution of peptides in the solvent and preferential ionization of more hydrophilic peptides in the mixture. Consequently, only MBM provided a complete tryptic map of β-amyloid (1–42) compared to 67% coverage by traditional MALDI. Acetonitrile (0.1% TFA) led to improved coverage only at a 50% molar ratio of peptide (1–42), but also to a side product of (1–42), Met oxidation (amino acid 35), a phenomenon not observed in MBM MALDI analysis. 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Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances

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