Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies

In this study, we investigated the interaction behavior of biodegradable, cationic, oxy-diester functionalized gemini surfactants N 1 ,N 1 ,N 14...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Akram, Mohd. [verfasserIn] Osama, Mohammad [verfasserIn] Lal, Hira [verfasserIn] Hashmi, Md. Amiruddin [verfasserIn] Anwar, Sana [verfasserIn] Kabir-ud-Din [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	C Hemoglobin Protein-surfactant binding Spectroscopy Docking MD simulation

Übergeordnetes Werk:	Enthalten in: Colloids and surfaces / A - Amsterdam [u.a.] : Elsevier Science, 1993, 675
Übergeordnetes Werk:	volume:675

DOI / URN:	10.1016/j.colsurfa.2023.132066

Katalog-ID:	ELV061822078

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245	1	0	\|a Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies
264		1	\|c 2023
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520			\|a In this study, we investigated the interaction behavior of biodegradable, cationic, oxy-diester functionalized gemini surfactants N 1 ,N 1 ,N 14 ,N 14 -tetramethyl-2,13-dioxo-N 1 ,N 14 -dialkyl-3,6,12-tetraoxateradecane-1,14-diaminium dichloride (in short Cm-E2O2-Cm, m = 12, 14 or 16 is the number of carbon atoms in the alkyl chain) with one of the most important proteins in red blood cells viz. hemoglobin. We employed a variety of in-vitro and in-silico methodologies, such as fluorescence, UV–vis, FT-IR and circular dichroism spectroscopies, DFT, molecular docking, and molecular dynamics simulations, to study these interactions. Our results show that the chain length of the surfactants have distinct implications for the interaction behavior, as evidenced by the estimated physical parameters, such as K b and ∆G. The order of K b values (0.24 × 103 < 3.11 ×103 < 5.85 × 103 M-1) is in accordance with the increasing alkyl chain length of the surfactants. The negative Gibbs free energy change values and their order, − 13.58 < −19.93 < −21.49, further support the spontaneity of interactions and the effect of alkyl chain length. Theoretical insight into the environment at the quantum mechanical level, binding site, and energy stability of the protein-surfactant interactions were produced by computational methods. This research contributes significantly to the field of knowledge concerning surfactants' effects on protein structure and behavior.
650		4	\|a C
650		4	\|a Hemoglobin
650		4	\|a Protein-surfactant binding
650		4	\|a Spectroscopy
650		4	\|a Docking
650		4	\|a MD simulation
700	1		\|a Osama, Mohammad \|e verfasserin \|0 (orcid)0000-0003-3978-647X \|4 aut
700	1		\|a Lal, Hira \|e verfasserin \|0 (orcid)0000-0002-9546-4128 \|4 aut
700	1		\|a Hashmi, Md. Amiruddin \|e verfasserin \|4 aut
700	1		\|a Anwar, Sana \|e verfasserin \|0 (orcid)0009-0006-4801-9132 \|4 aut
700	1		\|a Kabir-ud-Din \|e verfasserin \|4 aut
773	0	8	\|i Enthalten in \|t Colloids and surfaces / A \|d Amsterdam [u.a.] : Elsevier Science, 1993 \|g 675 \|h Online-Ressource \|w (DE-627)306659956 \|w (DE-600)1500517-3 \|w (DE-576)098614843 \|x 1873-4359 \|7 nnns
773	1	8	\|g volume:675
912			\|a GBV_USEFLAG_U
912			\|a GBV_ELV
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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_40
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
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_90
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_150
912			\|a GBV_ILN_151
912			\|a GBV_ILN_187
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
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_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_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
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2411
912			\|a GBV_ILN_2470
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4242
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_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
936	b	k	\|a 35.18 \|j Kolloidchemie \|j Grenzflächenchemie \|q VZ
936	b	k	\|a 33.68 \|j Oberflächen \|j Dünne Schichten \|j Grenzflächen \|x Physik \|q VZ
936	b	k	\|a 52.78 \|j Oberflächentechnik \|j Wärmebehandlung \|q VZ
936	b	k	\|a 58.20 \|j Chemische Technologien: Allgemeines \|q VZ
951			\|a AR
952			\|d 675

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bklnumber	35.18 33.68 52.78 58.20
publishDate	2023
allfields	10.1016/j.colsurfa.2023.132066 doi (DE-627)ELV061822078 (ELSEVIER)S0927-7757(23)01150-0 DE-627 ger DE-627 rda eng 540 VZ 35.18 bkl 33.68 bkl 52.78 bkl 58.20 bkl Akram, Mohd. verfasserin aut Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier In this study, we investigated the interaction behavior of biodegradable, cationic, oxy-diester functionalized gemini surfactants N 1 ,N 1 ,N 14 ,N 14 -tetramethyl-2,13-dioxo-N 1 ,N 14 -dialkyl-3,6,12-tetraoxateradecane-1,14-diaminium dichloride (in short Cm-E2O2-Cm, m = 12, 14 or 16 is the number of carbon atoms in the alkyl chain) with one of the most important proteins in red blood cells viz. hemoglobin. We employed a variety of in-vitro and in-silico methodologies, such as fluorescence, UV–vis, FT-IR and circular dichroism spectroscopies, DFT, molecular docking, and molecular dynamics simulations, to study these interactions. Our results show that the chain length of the surfactants have distinct implications for the interaction behavior, as evidenced by the estimated physical parameters, such as K b and ∆G. The order of K b values (0.24 × 103 < 3.11 ×103 < 5.85 × 103 M-1) is in accordance with the increasing alkyl chain length of the surfactants. The negative Gibbs free energy change values and their order, − 13.58 < −19.93 < −21.49, further support the spontaneity of interactions and the effect of alkyl chain length. Theoretical insight into the environment at the quantum mechanical level, binding site, and energy stability of the protein-surfactant interactions were produced by computational methods. This research contributes significantly to the field of knowledge concerning surfactants' effects on protein structure and behavior. C Hemoglobin Protein-surfactant binding Spectroscopy Docking MD simulation Osama, Mohammad verfasserin (orcid)0000-0003-3978-647X aut Lal, Hira verfasserin (orcid)0000-0002-9546-4128 aut Hashmi, Md. Amiruddin verfasserin aut Anwar, Sana verfasserin (orcid)0009-0006-4801-9132 aut Kabir-ud-Din verfasserin aut Enthalten in Colloids and surfaces / A Amsterdam [u.a.] : Elsevier Science, 1993 675 Online-Ressource (DE-627)306659956 (DE-600)1500517-3 (DE-576)098614843 1873-4359 nnns volume:675 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_2411 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 35.18 Kolloidchemie Grenzflächenchemie VZ 33.68 Oberflächen Dünne Schichten Grenzflächen Physik VZ 52.78 Oberflächentechnik Wärmebehandlung VZ 58.20 Chemische Technologien: Allgemeines VZ AR 675
spelling	10.1016/j.colsurfa.2023.132066 doi (DE-627)ELV061822078 (ELSEVIER)S0927-7757(23)01150-0 DE-627 ger DE-627 rda eng 540 VZ 35.18 bkl 33.68 bkl 52.78 bkl 58.20 bkl Akram, Mohd. verfasserin aut Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier In this study, we investigated the interaction behavior of biodegradable, cationic, oxy-diester functionalized gemini surfactants N 1 ,N 1 ,N 14 ,N 14 -tetramethyl-2,13-dioxo-N 1 ,N 14 -dialkyl-3,6,12-tetraoxateradecane-1,14-diaminium dichloride (in short Cm-E2O2-Cm, m = 12, 14 or 16 is the number of carbon atoms in the alkyl chain) with one of the most important proteins in red blood cells viz. hemoglobin. We employed a variety of in-vitro and in-silico methodologies, such as fluorescence, UV–vis, FT-IR and circular dichroism spectroscopies, DFT, molecular docking, and molecular dynamics simulations, to study these interactions. Our results show that the chain length of the surfactants have distinct implications for the interaction behavior, as evidenced by the estimated physical parameters, such as K b and ∆G. The order of K b values (0.24 × 103 < 3.11 ×103 < 5.85 × 103 M-1) is in accordance with the increasing alkyl chain length of the surfactants. The negative Gibbs free energy change values and their order, − 13.58 < −19.93 < −21.49, further support the spontaneity of interactions and the effect of alkyl chain length. Theoretical insight into the environment at the quantum mechanical level, binding site, and energy stability of the protein-surfactant interactions were produced by computational methods. This research contributes significantly to the field of knowledge concerning surfactants' effects on protein structure and behavior. C Hemoglobin Protein-surfactant binding Spectroscopy Docking MD simulation Osama, Mohammad verfasserin (orcid)0000-0003-3978-647X aut Lal, Hira verfasserin (orcid)0000-0002-9546-4128 aut Hashmi, Md. Amiruddin verfasserin aut Anwar, Sana verfasserin (orcid)0009-0006-4801-9132 aut Kabir-ud-Din verfasserin aut Enthalten in Colloids and surfaces / A Amsterdam [u.a.] : Elsevier Science, 1993 675 Online-Ressource (DE-627)306659956 (DE-600)1500517-3 (DE-576)098614843 1873-4359 nnns volume:675 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_2411 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 35.18 Kolloidchemie Grenzflächenchemie VZ 33.68 Oberflächen Dünne Schichten Grenzflächen Physik VZ 52.78 Oberflächentechnik Wärmebehandlung VZ 58.20 Chemische Technologien: Allgemeines VZ AR 675
allfields_unstemmed	10.1016/j.colsurfa.2023.132066 doi (DE-627)ELV061822078 (ELSEVIER)S0927-7757(23)01150-0 DE-627 ger DE-627 rda eng 540 VZ 35.18 bkl 33.68 bkl 52.78 bkl 58.20 bkl Akram, Mohd. verfasserin aut Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier In this study, we investigated the interaction behavior of biodegradable, cationic, oxy-diester functionalized gemini surfactants N 1 ,N 1 ,N 14 ,N 14 -tetramethyl-2,13-dioxo-N 1 ,N 14 -dialkyl-3,6,12-tetraoxateradecane-1,14-diaminium dichloride (in short Cm-E2O2-Cm, m = 12, 14 or 16 is the number of carbon atoms in the alkyl chain) with one of the most important proteins in red blood cells viz. hemoglobin. We employed a variety of in-vitro and in-silico methodologies, such as fluorescence, UV–vis, FT-IR and circular dichroism spectroscopies, DFT, molecular docking, and molecular dynamics simulations, to study these interactions. Our results show that the chain length of the surfactants have distinct implications for the interaction behavior, as evidenced by the estimated physical parameters, such as K b and ∆G. The order of K b values (0.24 × 103 < 3.11 ×103 < 5.85 × 103 M-1) is in accordance with the increasing alkyl chain length of the surfactants. The negative Gibbs free energy change values and their order, − 13.58 < −19.93 < −21.49, further support the spontaneity of interactions and the effect of alkyl chain length. Theoretical insight into the environment at the quantum mechanical level, binding site, and energy stability of the protein-surfactant interactions were produced by computational methods. This research contributes significantly to the field of knowledge concerning surfactants' effects on protein structure and behavior. C Hemoglobin Protein-surfactant binding Spectroscopy Docking MD simulation Osama, Mohammad verfasserin (orcid)0000-0003-3978-647X aut Lal, Hira verfasserin (orcid)0000-0002-9546-4128 aut Hashmi, Md. Amiruddin verfasserin aut Anwar, Sana verfasserin (orcid)0009-0006-4801-9132 aut Kabir-ud-Din verfasserin aut Enthalten in Colloids and surfaces / A Amsterdam [u.a.] : Elsevier Science, 1993 675 Online-Ressource (DE-627)306659956 (DE-600)1500517-3 (DE-576)098614843 1873-4359 nnns volume:675 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_2411 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 35.18 Kolloidchemie Grenzflächenchemie VZ 33.68 Oberflächen Dünne Schichten Grenzflächen Physik VZ 52.78 Oberflächentechnik Wärmebehandlung VZ 58.20 Chemische Technologien: Allgemeines VZ AR 675
allfieldsGer	10.1016/j.colsurfa.2023.132066 doi (DE-627)ELV061822078 (ELSEVIER)S0927-7757(23)01150-0 DE-627 ger DE-627 rda eng 540 VZ 35.18 bkl 33.68 bkl 52.78 bkl 58.20 bkl Akram, Mohd. verfasserin aut Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier In this study, we investigated the interaction behavior of biodegradable, cationic, oxy-diester functionalized gemini surfactants N 1 ,N 1 ,N 14 ,N 14 -tetramethyl-2,13-dioxo-N 1 ,N 14 -dialkyl-3,6,12-tetraoxateradecane-1,14-diaminium dichloride (in short Cm-E2O2-Cm, m = 12, 14 or 16 is the number of carbon atoms in the alkyl chain) with one of the most important proteins in red blood cells viz. hemoglobin. We employed a variety of in-vitro and in-silico methodologies, such as fluorescence, UV–vis, FT-IR and circular dichroism spectroscopies, DFT, molecular docking, and molecular dynamics simulations, to study these interactions. Our results show that the chain length of the surfactants have distinct implications for the interaction behavior, as evidenced by the estimated physical parameters, such as K b and ∆G. The order of K b values (0.24 × 103 < 3.11 ×103 < 5.85 × 103 M-1) is in accordance with the increasing alkyl chain length of the surfactants. The negative Gibbs free energy change values and their order, − 13.58 < −19.93 < −21.49, further support the spontaneity of interactions and the effect of alkyl chain length. Theoretical insight into the environment at the quantum mechanical level, binding site, and energy stability of the protein-surfactant interactions were produced by computational methods. This research contributes significantly to the field of knowledge concerning surfactants' effects on protein structure and behavior. C Hemoglobin Protein-surfactant binding Spectroscopy Docking MD simulation Osama, Mohammad verfasserin (orcid)0000-0003-3978-647X aut Lal, Hira verfasserin (orcid)0000-0002-9546-4128 aut Hashmi, Md. Amiruddin verfasserin aut Anwar, Sana verfasserin (orcid)0009-0006-4801-9132 aut Kabir-ud-Din verfasserin aut Enthalten in Colloids and surfaces / A Amsterdam [u.a.] : Elsevier Science, 1993 675 Online-Ressource (DE-627)306659956 (DE-600)1500517-3 (DE-576)098614843 1873-4359 nnns volume:675 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_2411 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 35.18 Kolloidchemie Grenzflächenchemie VZ 33.68 Oberflächen Dünne Schichten Grenzflächen Physik VZ 52.78 Oberflächentechnik Wärmebehandlung VZ 58.20 Chemische Technologien: Allgemeines VZ AR 675
allfieldsSound	10.1016/j.colsurfa.2023.132066 doi (DE-627)ELV061822078 (ELSEVIER)S0927-7757(23)01150-0 DE-627 ger DE-627 rda eng 540 VZ 35.18 bkl 33.68 bkl 52.78 bkl 58.20 bkl Akram, Mohd. verfasserin aut Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier In this study, we investigated the interaction behavior of biodegradable, cationic, oxy-diester functionalized gemini surfactants N 1 ,N 1 ,N 14 ,N 14 -tetramethyl-2,13-dioxo-N 1 ,N 14 -dialkyl-3,6,12-tetraoxateradecane-1,14-diaminium dichloride (in short Cm-E2O2-Cm, m = 12, 14 or 16 is the number of carbon atoms in the alkyl chain) with one of the most important proteins in red blood cells viz. hemoglobin. We employed a variety of in-vitro and in-silico methodologies, such as fluorescence, UV–vis, FT-IR and circular dichroism spectroscopies, DFT, molecular docking, and molecular dynamics simulations, to study these interactions. Our results show that the chain length of the surfactants have distinct implications for the interaction behavior, as evidenced by the estimated physical parameters, such as K b and ∆G. The order of K b values (0.24 × 103 < 3.11 ×103 < 5.85 × 103 M-1) is in accordance with the increasing alkyl chain length of the surfactants. The negative Gibbs free energy change values and their order, − 13.58 < −19.93 < −21.49, further support the spontaneity of interactions and the effect of alkyl chain length. Theoretical insight into the environment at the quantum mechanical level, binding site, and energy stability of the protein-surfactant interactions were produced by computational methods. This research contributes significantly to the field of knowledge concerning surfactants' effects on protein structure and behavior. C Hemoglobin Protein-surfactant binding Spectroscopy Docking MD simulation Osama, Mohammad verfasserin (orcid)0000-0003-3978-647X aut Lal, Hira verfasserin (orcid)0000-0002-9546-4128 aut Hashmi, Md. Amiruddin verfasserin aut Anwar, Sana verfasserin (orcid)0009-0006-4801-9132 aut Kabir-ud-Din verfasserin aut Enthalten in Colloids and surfaces / A Amsterdam [u.a.] : Elsevier Science, 1993 675 Online-Ressource (DE-627)306659956 (DE-600)1500517-3 (DE-576)098614843 1873-4359 nnns volume:675 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_2411 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 35.18 Kolloidchemie Grenzflächenchemie VZ 33.68 Oberflächen Dünne Schichten Grenzflächen Physik VZ 52.78 Oberflächentechnik Wärmebehandlung VZ 58.20 Chemische Technologien: Allgemeines VZ AR 675
language	English
source	Enthalten in Colloids and surfaces / A 675 volume:675
sourceStr	Enthalten in Colloids and surfaces / A 675 volume:675
format_phy_str_mv	Article
bklname	Kolloidchemie Grenzflächenchemie Oberflächen Dünne Schichten Grenzflächen Oberflächentechnik Wärmebehandlung Chemische Technologien: Allgemeines
institution	findex.gbv.de
topic_facet	C Hemoglobin Protein-surfactant binding Spectroscopy Docking MD simulation
dewey-raw	540
isfreeaccess_bool	false
container_title	Colloids and surfaces / A
authorswithroles_txt_mv	Akram, Mohd. @@aut@@ Osama, Mohammad @@aut@@ Lal, Hira @@aut@@ Hashmi, Md. Amiruddin @@aut@@ Anwar, Sana @@aut@@ Kabir-ud-Din @@aut@@
publishDateDaySort_date	2023-01-01T00:00:00Z
hierarchy_top_id	306659956
dewey-sort	3540
id	ELV061822078
language_de	englisch
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spellingShingle	Akram, Mohd. ddc 540 bkl 35.18 bkl 33.68 bkl 52.78 bkl 58.20 misc C misc Hemoglobin misc Protein-surfactant binding misc Spectroscopy misc Docking misc MD simulation Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies
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topic_title	540 VZ 35.18 bkl 33.68 bkl 52.78 bkl 58.20 bkl Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies C Hemoglobin Protein-surfactant binding Spectroscopy Docking MD simulation
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title	Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies
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title_full	Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies
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author_browse	Akram, Mohd. Osama, Mohammad Lal, Hira Hashmi, Md. Amiruddin Anwar, Sana Kabir-ud-Din
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title_sort	physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: insights from spectroscopic and computational studies
title_auth	Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies
abstract	In this study, we investigated the interaction behavior of biodegradable, cationic, oxy-diester functionalized gemini surfactants N 1 ,N 1 ,N 14 ,N 14 -tetramethyl-2,13-dioxo-N 1 ,N 14 -dialkyl-3,6,12-tetraoxateradecane-1,14-diaminium dichloride (in short Cm-E2O2-Cm, m = 12, 14 or 16 is the number of carbon atoms in the alkyl chain) with one of the most important proteins in red blood cells viz. hemoglobin. We employed a variety of in-vitro and in-silico methodologies, such as fluorescence, UV–vis, FT-IR and circular dichroism spectroscopies, DFT, molecular docking, and molecular dynamics simulations, to study these interactions. Our results show that the chain length of the surfactants have distinct implications for the interaction behavior, as evidenced by the estimated physical parameters, such as K b and ∆G. The order of K b values (0.24 × 103 < 3.11 ×103 < 5.85 × 103 M-1) is in accordance with the increasing alkyl chain length of the surfactants. The negative Gibbs free energy change values and their order, − 13.58 < −19.93 < −21.49, further support the spontaneity of interactions and the effect of alkyl chain length. Theoretical insight into the environment at the quantum mechanical level, binding site, and energy stability of the protein-surfactant interactions were produced by computational methods. This research contributes significantly to the field of knowledge concerning surfactants' effects on protein structure and behavior.
abstractGer	In this study, we investigated the interaction behavior of biodegradable, cationic, oxy-diester functionalized gemini surfactants N 1 ,N 1 ,N 14 ,N 14 -tetramethyl-2,13-dioxo-N 1 ,N 14 -dialkyl-3,6,12-tetraoxateradecane-1,14-diaminium dichloride (in short Cm-E2O2-Cm, m = 12, 14 or 16 is the number of carbon atoms in the alkyl chain) with one of the most important proteins in red blood cells viz. hemoglobin. We employed a variety of in-vitro and in-silico methodologies, such as fluorescence, UV–vis, FT-IR and circular dichroism spectroscopies, DFT, molecular docking, and molecular dynamics simulations, to study these interactions. Our results show that the chain length of the surfactants have distinct implications for the interaction behavior, as evidenced by the estimated physical parameters, such as K b and ∆G. The order of K b values (0.24 × 103 < 3.11 ×103 < 5.85 × 103 M-1) is in accordance with the increasing alkyl chain length of the surfactants. The negative Gibbs free energy change values and their order, − 13.58 < −19.93 < −21.49, further support the spontaneity of interactions and the effect of alkyl chain length. Theoretical insight into the environment at the quantum mechanical level, binding site, and energy stability of the protein-surfactant interactions were produced by computational methods. This research contributes significantly to the field of knowledge concerning surfactants' effects on protein structure and behavior.
abstract_unstemmed	In this study, we investigated the interaction behavior of biodegradable, cationic, oxy-diester functionalized gemini surfactants N 1 ,N 1 ,N 14 ,N 14 -tetramethyl-2,13-dioxo-N 1 ,N 14 -dialkyl-3,6,12-tetraoxateradecane-1,14-diaminium dichloride (in short Cm-E2O2-Cm, m = 12, 14 or 16 is the number of carbon atoms in the alkyl chain) with one of the most important proteins in red blood cells viz. hemoglobin. We employed a variety of in-vitro and in-silico methodologies, such as fluorescence, UV–vis, FT-IR and circular dichroism spectroscopies, DFT, molecular docking, and molecular dynamics simulations, to study these interactions. Our results show that the chain length of the surfactants have distinct implications for the interaction behavior, as evidenced by the estimated physical parameters, such as K b and ∆G. The order of K b values (0.24 × 103 < 3.11 ×103 < 5.85 × 103 M-1) is in accordance with the increasing alkyl chain length of the surfactants. The negative Gibbs free energy change values and their order, − 13.58 < −19.93 < −21.49, further support the spontaneity of interactions and the effect of alkyl chain length. Theoretical insight into the environment at the quantum mechanical level, binding site, and energy stability of the protein-surfactant interactions were produced by computational methods. This research contributes significantly to the field of knowledge concerning surfactants' effects on protein structure and behavior.
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title_short	Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies
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author2	Osama, Mohammad Lal, Hira Hashmi, Md. Amiruddin Anwar, Sana Kabir-ud-Din
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doi_str	10.1016/j.colsurfa.2023.132066
up_date	2024-07-06T18:05:39.009Z
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We employed a variety of in-vitro and in-silico methodologies, such as fluorescence, UV–vis, FT-IR and circular dichroism spectroscopies, DFT, molecular docking, and molecular dynamics simulations, to study these interactions. Our results show that the chain length of the surfactants have distinct implications for the interaction behavior, as evidenced by the estimated physical parameters, such as K b and ∆G. The order of K b values (0.24 × 103 < 3.11 ×103 < 5.85 × 103 M-1) is in accordance with the increasing alkyl chain length of the surfactants. The negative Gibbs free energy change values and their order, − 13.58 < −19.93 < −21.49, further support the spontaneity of interactions and the effect of alkyl chain length. Theoretical insight into the environment at the quantum mechanical level, binding site, and energy stability of the protein-surfactant interactions were produced by computational methods. 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Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies

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