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Single-molecule analysis of osmolyte-mediated nanomechanical unfolding behavior of a protein domain

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Single-molecule analysis of osmolyte-mediated nanomechanical unfolding behavior of a protein domain
 
Creator Bajaj, Manish
Muddassir, Mohd
Choi, Bumjoon
Singh, Priyanka
Park, Jong Bum
Singh, Surjeet
Yadav, Manisha
Kumar, Rajesh
Eom, Kilho
Sharma, Deepak
 
Subject QR Microbiology
 
Description The small organic molecules, known as osmolytes being ubiquitously present in different cell types, affect protein folding, stability and aggregation. However, it is unknown how the osmolytes affect the nanomechanical unfolding behavior of protein domain. Here, we show the osmolyte-dependent mechanical unfolding properties of protein titin immunoglobulin-27 (I27) domain using an atomic force microscopy (AFM)-based single-molecule force spectroscopy. We found that amines and methylamines improved the mechanical stability of I27 domain, whereas polyols had no effect. Interestingly, glycine betaine (GB) or trimethylamine-N-oxide (TMAO) increased the average unfolding force of the protein domain. The kinetic parameters analyzed at single-molecule level reveal that stabilizing effect of osmolytes is due to a decrease in the unfolding rate constant of I27, which was confirmed by molecular dynamics simulations. Our study reveals different effects that diverse osmolytes have on the mechanical properties of the protein, and suggests the potential use of osmolytes in modulating the mechanical stability of proteins required for various nano-biotechnological applications.
 
Publisher Elsevier Science
 
Date 2023-12-31
 
Type Article
PeerReviewed
 
Relation https://www.sciencedirect.com/science/article/pii/S0141813023037467?via%3Dihub
http://crdd.osdd.net/open/3162/
 
Identifier Bajaj, Manish and Muddassir, Mohd and Choi, Bumjoon and Singh, Priyanka and Park, Jong Bum and Singh, Surjeet and Yadav, Manisha and Kumar, Rajesh and Eom, Kilho and Sharma, Deepak (2023) Single-molecule analysis of osmolyte-mediated nanomechanical unfolding behavior of a protein domain. International journal of biological macromolecules, 253. ISSN 1879-0003