Coiled-coil scallops

Self-assembly of peptides is a powerful method of preparing nanostructured materials. Peptides frequently utilize charged groups as a convenient switch for controlling assembly state by pH, ionic strength or temperature. In this study, the molecular properties and gel-forming ability of Chlamys farr...
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Autor*in:	Wu, Di [verfasserIn] Wu, Chao [verfasserIn] Ma, Wuchao [verfasserIn] Wang, Zhenyu [verfasserIn] Yang, Meilian [verfasserIn] El-Seedi, Hesham R. [verfasserIn] Du, Ming [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	Peptide Self-assembly Hydrogel Ionic responsive Temperature responsive

Übergeordnetes Werk:	Enthalten in: Food chemistry - New York, NY [u.a.] : Elsevier, 1976, 433
Übergeordnetes Werk:	volume:433

DOI / URN:	10.1016/j.foodchem.2023.137230

Katalog-ID:	ELV064964450

Internformat


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520			\|a Self-assembly of peptides is a powerful method of preparing nanostructured materials. Peptides frequently utilize charged groups as a convenient switch for controlling assembly state by pH, ionic strength or temperature. In this study, the molecular properties and gel-forming ability of Chlamys farreri protein hydrolysates were studied. According to self-assembled theory, the presence of isoleucine at position ‘a’ and leucine at ‘d’ causes a switch between coiled-coil structures. Compared to P-2-CG, the components of α-helix (23.60 ± 0.56%) were changed into β-sheet (4.83 ± 2.86%) in the secondary structure of the hydrogel induced by ZnCl2. NMR siginals appeared at high field,which indicated hydrogen bonds were formed between P-2-CG and solvent environments at 20 °C. With temperature going up, the hydrogen bonds were broken and nanofibrils were changed into dense aggregates. We expected that P-2-CG could provide a new candidate for preparing metal-induced nanofibers or hydrogels with further applications in food industry.
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650		4	\|a Self-assembly
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650		4	\|a Temperature responsive
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700	1		\|a Ma, Wuchao \|e verfasserin \|4 aut
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700	1		\|a Yang, Meilian \|e verfasserin \|4 aut
700	1		\|a El-Seedi, Hesham R. \|e verfasserin \|4 aut
700	1		\|a Du, Ming \|e verfasserin \|0 (orcid)0000-0001-5872-8529 \|4 aut
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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_2034
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
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
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912			\|a GBV_ILN_2106
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912			\|a GBV_ILN_2507
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
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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_4326
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4393
912			\|a GBV_ILN_4700
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author_variant	d w dw c w cw w m wm z w zw m y my h r e s hre hres m d md
matchkey_str	article:18737072:2023----::oldolc
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bklnumber	58.34
publishDate	2023
allfields	10.1016/j.foodchem.2023.137230 doi (DE-627)ELV064964450 (ELSEVIER)S0308-8146(23)01848-4 DE-627 ger DE-627 rda eng 540 660 VZ 58.34 bkl Wu, Di verfasserin aut Coiled-coil scallops 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Self-assembly of peptides is a powerful method of preparing nanostructured materials. Peptides frequently utilize charged groups as a convenient switch for controlling assembly state by pH, ionic strength or temperature. In this study, the molecular properties and gel-forming ability of Chlamys farreri protein hydrolysates were studied. According to self-assembled theory, the presence of isoleucine at position ‘a’ and leucine at ‘d’ causes a switch between coiled-coil structures. Compared to P-2-CG, the components of α-helix (23.60 ± 0.56%) were changed into β-sheet (4.83 ± 2.86%) in the secondary structure of the hydrogel induced by ZnCl2. NMR siginals appeared at high field,which indicated hydrogen bonds were formed between P-2-CG and solvent environments at 20 °C. With temperature going up, the hydrogen bonds were broken and nanofibrils were changed into dense aggregates. We expected that P-2-CG could provide a new candidate for preparing metal-induced nanofibers or hydrogels with further applications in food industry. Peptide Self-assembly Hydrogel Ionic responsive Temperature responsive Wu, Chao verfasserin aut Ma, Wuchao verfasserin aut Wang, Zhenyu verfasserin aut Yang, Meilian verfasserin aut El-Seedi, Hesham R. verfasserin aut Du, Ming verfasserin (orcid)0000-0001-5872-8529 aut Enthalten in Food chemistry New York, NY [u.a.] : Elsevier, 1976 433 Online-Ressource (DE-627)300898509 (DE-600)1483647-6 (DE-576)098330225 1873-7072 nnns volume:433 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 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_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.34 Lebensmitteltechnologie VZ AR 433
spelling	10.1016/j.foodchem.2023.137230 doi (DE-627)ELV064964450 (ELSEVIER)S0308-8146(23)01848-4 DE-627 ger DE-627 rda eng 540 660 VZ 58.34 bkl Wu, Di verfasserin aut Coiled-coil scallops 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Self-assembly of peptides is a powerful method of preparing nanostructured materials. Peptides frequently utilize charged groups as a convenient switch for controlling assembly state by pH, ionic strength or temperature. In this study, the molecular properties and gel-forming ability of Chlamys farreri protein hydrolysates were studied. According to self-assembled theory, the presence of isoleucine at position ‘a’ and leucine at ‘d’ causes a switch between coiled-coil structures. Compared to P-2-CG, the components of α-helix (23.60 ± 0.56%) were changed into β-sheet (4.83 ± 2.86%) in the secondary structure of the hydrogel induced by ZnCl2. NMR siginals appeared at high field,which indicated hydrogen bonds were formed between P-2-CG and solvent environments at 20 °C. With temperature going up, the hydrogen bonds were broken and nanofibrils were changed into dense aggregates. We expected that P-2-CG could provide a new candidate for preparing metal-induced nanofibers or hydrogels with further applications in food industry. Peptide Self-assembly Hydrogel Ionic responsive Temperature responsive Wu, Chao verfasserin aut Ma, Wuchao verfasserin aut Wang, Zhenyu verfasserin aut Yang, Meilian verfasserin aut El-Seedi, Hesham R. verfasserin aut Du, Ming verfasserin (orcid)0000-0001-5872-8529 aut Enthalten in Food chemistry New York, NY [u.a.] : Elsevier, 1976 433 Online-Ressource (DE-627)300898509 (DE-600)1483647-6 (DE-576)098330225 1873-7072 nnns volume:433 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 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_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.34 Lebensmitteltechnologie VZ AR 433
allfields_unstemmed	10.1016/j.foodchem.2023.137230 doi (DE-627)ELV064964450 (ELSEVIER)S0308-8146(23)01848-4 DE-627 ger DE-627 rda eng 540 660 VZ 58.34 bkl Wu, Di verfasserin aut Coiled-coil scallops 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Self-assembly of peptides is a powerful method of preparing nanostructured materials. Peptides frequently utilize charged groups as a convenient switch for controlling assembly state by pH, ionic strength or temperature. In this study, the molecular properties and gel-forming ability of Chlamys farreri protein hydrolysates were studied. According to self-assembled theory, the presence of isoleucine at position ‘a’ and leucine at ‘d’ causes a switch between coiled-coil structures. Compared to P-2-CG, the components of α-helix (23.60 ± 0.56%) were changed into β-sheet (4.83 ± 2.86%) in the secondary structure of the hydrogel induced by ZnCl2. NMR siginals appeared at high field,which indicated hydrogen bonds were formed between P-2-CG and solvent environments at 20 °C. With temperature going up, the hydrogen bonds were broken and nanofibrils were changed into dense aggregates. We expected that P-2-CG could provide a new candidate for preparing metal-induced nanofibers or hydrogels with further applications in food industry. Peptide Self-assembly Hydrogel Ionic responsive Temperature responsive Wu, Chao verfasserin aut Ma, Wuchao verfasserin aut Wang, Zhenyu verfasserin aut Yang, Meilian verfasserin aut El-Seedi, Hesham R. verfasserin aut Du, Ming verfasserin (orcid)0000-0001-5872-8529 aut Enthalten in Food chemistry New York, NY [u.a.] : Elsevier, 1976 433 Online-Ressource (DE-627)300898509 (DE-600)1483647-6 (DE-576)098330225 1873-7072 nnns volume:433 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 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_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.34 Lebensmitteltechnologie VZ AR 433
allfieldsGer	10.1016/j.foodchem.2023.137230 doi (DE-627)ELV064964450 (ELSEVIER)S0308-8146(23)01848-4 DE-627 ger DE-627 rda eng 540 660 VZ 58.34 bkl Wu, Di verfasserin aut Coiled-coil scallops 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Self-assembly of peptides is a powerful method of preparing nanostructured materials. Peptides frequently utilize charged groups as a convenient switch for controlling assembly state by pH, ionic strength or temperature. In this study, the molecular properties and gel-forming ability of Chlamys farreri protein hydrolysates were studied. According to self-assembled theory, the presence of isoleucine at position ‘a’ and leucine at ‘d’ causes a switch between coiled-coil structures. Compared to P-2-CG, the components of α-helix (23.60 ± 0.56%) were changed into β-sheet (4.83 ± 2.86%) in the secondary structure of the hydrogel induced by ZnCl2. NMR siginals appeared at high field,which indicated hydrogen bonds were formed between P-2-CG and solvent environments at 20 °C. With temperature going up, the hydrogen bonds were broken and nanofibrils were changed into dense aggregates. We expected that P-2-CG could provide a new candidate for preparing metal-induced nanofibers or hydrogels with further applications in food industry. Peptide Self-assembly Hydrogel Ionic responsive Temperature responsive Wu, Chao verfasserin aut Ma, Wuchao verfasserin aut Wang, Zhenyu verfasserin aut Yang, Meilian verfasserin aut El-Seedi, Hesham R. verfasserin aut Du, Ming verfasserin (orcid)0000-0001-5872-8529 aut Enthalten in Food chemistry New York, NY [u.a.] : Elsevier, 1976 433 Online-Ressource (DE-627)300898509 (DE-600)1483647-6 (DE-576)098330225 1873-7072 nnns volume:433 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 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_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.34 Lebensmitteltechnologie VZ AR 433
allfieldsSound	10.1016/j.foodchem.2023.137230 doi (DE-627)ELV064964450 (ELSEVIER)S0308-8146(23)01848-4 DE-627 ger DE-627 rda eng 540 660 VZ 58.34 bkl Wu, Di verfasserin aut Coiled-coil scallops 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Self-assembly of peptides is a powerful method of preparing nanostructured materials. Peptides frequently utilize charged groups as a convenient switch for controlling assembly state by pH, ionic strength or temperature. In this study, the molecular properties and gel-forming ability of Chlamys farreri protein hydrolysates were studied. According to self-assembled theory, the presence of isoleucine at position ‘a’ and leucine at ‘d’ causes a switch between coiled-coil structures. Compared to P-2-CG, the components of α-helix (23.60 ± 0.56%) were changed into β-sheet (4.83 ± 2.86%) in the secondary structure of the hydrogel induced by ZnCl2. NMR siginals appeared at high field,which indicated hydrogen bonds were formed between P-2-CG and solvent environments at 20 °C. With temperature going up, the hydrogen bonds were broken and nanofibrils were changed into dense aggregates. We expected that P-2-CG could provide a new candidate for preparing metal-induced nanofibers or hydrogels with further applications in food industry. Peptide Self-assembly Hydrogel Ionic responsive Temperature responsive Wu, Chao verfasserin aut Ma, Wuchao verfasserin aut Wang, Zhenyu verfasserin aut Yang, Meilian verfasserin aut El-Seedi, Hesham R. verfasserin aut Du, Ming verfasserin (orcid)0000-0001-5872-8529 aut Enthalten in Food chemistry New York, NY [u.a.] : Elsevier, 1976 433 Online-Ressource (DE-627)300898509 (DE-600)1483647-6 (DE-576)098330225 1873-7072 nnns volume:433 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 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_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.34 Lebensmitteltechnologie VZ AR 433
language	English
source	Enthalten in Food chemistry 433 volume:433
sourceStr	Enthalten in Food chemistry 433 volume:433
format_phy_str_mv	Article
bklname	Lebensmitteltechnologie
institution	findex.gbv.de
topic_facet	Peptide Self-assembly Hydrogel Ionic responsive Temperature responsive
dewey-raw	540
isfreeaccess_bool	false
container_title	Food chemistry
authorswithroles_txt_mv	Wu, Di @@aut@@ Wu, Chao @@aut@@ Ma, Wuchao @@aut@@ Wang, Zhenyu @@aut@@ Yang, Meilian @@aut@@ El-Seedi, Hesham R. @@aut@@ Du, Ming @@aut@@
publishDateDaySort_date	2023-01-01T00:00:00Z
hierarchy_top_id	300898509
dewey-sort	3540
id	ELV064964450
language_de	englisch
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topic_title	540 660 VZ 58.34 bkl Coiled-coil scallops Peptide Self-assembly Hydrogel Ionic responsive Temperature responsive
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title	Coiled-coil scallops
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title_sort	coiled-coil scallops
title_auth	Coiled-coil scallops
abstract	Self-assembly of peptides is a powerful method of preparing nanostructured materials. Peptides frequently utilize charged groups as a convenient switch for controlling assembly state by pH, ionic strength or temperature. In this study, the molecular properties and gel-forming ability of Chlamys farreri protein hydrolysates were studied. According to self-assembled theory, the presence of isoleucine at position ‘a’ and leucine at ‘d’ causes a switch between coiled-coil structures. Compared to P-2-CG, the components of α-helix (23.60 ± 0.56%) were changed into β-sheet (4.83 ± 2.86%) in the secondary structure of the hydrogel induced by ZnCl2. NMR siginals appeared at high field,which indicated hydrogen bonds were formed between P-2-CG and solvent environments at 20 °C. With temperature going up, the hydrogen bonds were broken and nanofibrils were changed into dense aggregates. We expected that P-2-CG could provide a new candidate for preparing metal-induced nanofibers or hydrogels with further applications in food industry.
abstractGer	Self-assembly of peptides is a powerful method of preparing nanostructured materials. Peptides frequently utilize charged groups as a convenient switch for controlling assembly state by pH, ionic strength or temperature. In this study, the molecular properties and gel-forming ability of Chlamys farreri protein hydrolysates were studied. According to self-assembled theory, the presence of isoleucine at position ‘a’ and leucine at ‘d’ causes a switch between coiled-coil structures. Compared to P-2-CG, the components of α-helix (23.60 ± 0.56%) were changed into β-sheet (4.83 ± 2.86%) in the secondary structure of the hydrogel induced by ZnCl2. NMR siginals appeared at high field,which indicated hydrogen bonds were formed between P-2-CG and solvent environments at 20 °C. With temperature going up, the hydrogen bonds were broken and nanofibrils were changed into dense aggregates. We expected that P-2-CG could provide a new candidate for preparing metal-induced nanofibers or hydrogels with further applications in food industry.
abstract_unstemmed	Self-assembly of peptides is a powerful method of preparing nanostructured materials. Peptides frequently utilize charged groups as a convenient switch for controlling assembly state by pH, ionic strength or temperature. In this study, the molecular properties and gel-forming ability of Chlamys farreri protein hydrolysates were studied. According to self-assembled theory, the presence of isoleucine at position ‘a’ and leucine at ‘d’ causes a switch between coiled-coil structures. Compared to P-2-CG, the components of α-helix (23.60 ± 0.56%) were changed into β-sheet (4.83 ± 2.86%) in the secondary structure of the hydrogel induced by ZnCl2. NMR siginals appeared at high field,which indicated hydrogen bonds were formed between P-2-CG and solvent environments at 20 °C. With temperature going up, the hydrogen bonds were broken and nanofibrils were changed into dense aggregates. We expected that P-2-CG could provide a new candidate for preparing metal-induced nanofibers or hydrogels with further applications in food industry.
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title_short	Coiled-coil scallops
remote_bool	true
author2	Wu, Chao Ma, Wuchao Wang, Zhenyu Yang, Meilian El-Seedi, Hesham R. Du, Ming
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doi_str	10.1016/j.foodchem.2023.137230
up_date	2024-07-06T21:21:00.894Z
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