Structural changes in trypsin induced by the bile salts : An effect of amphiphile hydrophobicity
Copyright © 2021. Published by Elsevier B.V..
The present study reports the multi-technique results of the interaction of a series of bile salts, sodium cholate (NaC), sodium taurocholate (NaTC), sodium deoxycholate (NaDC), and sodium taurodeoxycholate (NaTDC) with trypsin under the experimental conditions of 25 °C and pH 7.0. The interactions between trypsin and the bile salts were characterized by the surface tension measurements and various spectroscopic techniques like UV-Visible absorption, steady-state fluorescence, and circular dichroism. The results of surface tension measurements reveal a strong interaction of trypsin (50 μM) with the increasing concentration of bile salts, being higher with the bile salt of greater hydrophobicity. The critical aggregation concentration of bile salts in the presence of trypsin (C1) showed that the bile salts interact strongly with the trypsin in the order of NaTDC > NaDC > NaTC > NaC. UV-visible, steady-state fluorescence, and circular dichroism spectroscopic results confirmed significant unfolding of trypsin due to its interaction with the bile salts, the extent of which followed the same sequence as observed in the surface tension results. It could be concluded that the hydrophobic bile salts that show lower C1 values and have less delocalized charge, are more effective in unfolding the trypsin. The study would help understand the hydrophobicity-driven unfolding of proteins aided by biological surfactants like bile salts and help devise efficient proteolytic enzyme-based detergent formulations and understand the role of such amphiphiles as antimicrobial agents.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:180 |
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| Enthalten in: |
International journal of biological macromolecules - 180(2021) vom: 01. Juni, Seite 121-128 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Najar, Muzaffar Hussain [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 26.07.2021 Date Revised 26.07.2021 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.ijbiomac.2021.03.041 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM322705894 |
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| 100 | 1 | |a Najar, Muzaffar Hussain |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Structural changes in trypsin induced by the bile salts |b An effect of amphiphile hydrophobicity |
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| 500 | |a Date Revised 26.07.2021 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2021. Published by Elsevier B.V. | ||
| 520 | |a The present study reports the multi-technique results of the interaction of a series of bile salts, sodium cholate (NaC), sodium taurocholate (NaTC), sodium deoxycholate (NaDC), and sodium taurodeoxycholate (NaTDC) with trypsin under the experimental conditions of 25 °C and pH 7.0. The interactions between trypsin and the bile salts were characterized by the surface tension measurements and various spectroscopic techniques like UV-Visible absorption, steady-state fluorescence, and circular dichroism. The results of surface tension measurements reveal a strong interaction of trypsin (50 μM) with the increasing concentration of bile salts, being higher with the bile salt of greater hydrophobicity. The critical aggregation concentration of bile salts in the presence of trypsin (C1) showed that the bile salts interact strongly with the trypsin in the order of NaTDC > NaDC > NaTC > NaC. UV-visible, steady-state fluorescence, and circular dichroism spectroscopic results confirmed significant unfolding of trypsin due to its interaction with the bile salts, the extent of which followed the same sequence as observed in the surface tension results. It could be concluded that the hydrophobic bile salts that show lower C1 values and have less delocalized charge, are more effective in unfolding the trypsin. The study would help understand the hydrophobicity-driven unfolding of proteins aided by biological surfactants like bile salts and help devise efficient proteolytic enzyme-based detergent formulations and understand the role of such amphiphiles as antimicrobial agents | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Bile salts | |
| 650 | 4 | |a Circular dichroism | |
| 650 | 4 | |a Fluorescence | |
| 650 | 4 | |a Tensiometry | |
| 650 | 4 | |a Trypsin | |
| 650 | 7 | |a Ligands |2 NLM | |
| 650 | 7 | |a Micelles |2 NLM | |
| 650 | 7 | |a Surface-Active Agents |2 NLM | |
| 650 | 7 | |a Taurodeoxycholic Acid |2 NLM | |
| 650 | 7 | |a 516-50-7 |2 NLM | |
| 650 | 7 | |a Taurocholic Acid |2 NLM | |
| 650 | 7 | |a 5E090O0G3Z |2 NLM | |
| 650 | 7 | |a Trypsin |2 NLM | |
| 650 | 7 | |a EC 3.4.21.4 |2 NLM | |
| 650 | 7 | |a Sodium Cholate |2 NLM | |
| 650 | 7 | |a NU3Y4CCH8Z |2 NLM | |
| 700 | 1 | |a Chat, Oyais Ahmad |e verfasserin |4 aut | |
| 700 | 1 | |a Bhat, Parvaiz Ahmad |e verfasserin |4 aut | |
| 700 | 1 | |a Mir, Mohammad Amin |e verfasserin |4 aut | |
| 700 | 1 | |a Rather, Ghulam Mohamamd |e verfasserin |4 aut | |
| 700 | 1 | |a Dar, Aijaz Ahmad |e verfasserin |4 aut | |
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