Specific binding at the cellulose binding module-cellulose interface observed by force spectroscopy

Langmuir : the ACS Journal of Surfaces and Colloids
Jason R KingEric J Toone

Abstract

The need for effective enzymatic depolymerization of cellulose has stimulated an interest in interactions between protein and cellulose. Techniques utilized for quantitative measurements of protein-cellulose noncovalent association include microgravimetry, calorimetry, and atomic force microscopy (AFM), none of which differentiate between specific protein-cellulose binding and nonspecific adhesion. Here, we describe an AFM approach that differentiates nonspecific from specific interactions between cellulose-binding modules (CBMs) and cellulose. We demonstrate that the "mismatched" interaction between murine galectin-3, a lectin with no known affinity for cellulose, and cellulose shows molecular recognition force microscopy profiles similar to those observed during the interaction of a "matched" clostridial CBM3a with the same substrate. We also examine differences in binding probabilities and rupture profiles during CBM-cellulose binding experiments in the presence and absence of a blocking agent-a substrate specific for CBM that presumably blocks binding sites. By comparison of the behavior of the two proteins, we separate specific (i.e., blockable) and nonspecific adhesion events and show that both classes of interaction exhi...Continue Reading

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Citations

Jan 11, 2016·Advanced Materials·Melissabye GunnooDamien Thompson
Jun 14, 2018·Frontiers in Microbiology·Matthias FrommhagenMirjam A Kabel
Aug 30, 2020·Nature Communications·Zhaowei LiuMichael A Nash
Apr 2, 2020·Biomaterials Science·Albert Galera-PratMariano Carrión-Vázquez
Jan 19, 2019·Biomacromolecules·Alessandra GriffoPäivi Laaksonen

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