期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 19, 期 3, 页码 -出版社
MDPI
DOI: 10.3390/ijms19030840
关键词
nanocellulose; protease sensor; human neutrophil elastase; peptide-cellulose conformation; aerogel
资金
- U.S. Department of Agriculture
- project CAPBONE by Austrian Science Fund
Nanocellulose has high specific surface area, hydration properties, and ease of derivatization to prepare protease sensors. A Human Neutrophil Elastase sensor designed with a nanocellulose aerogel transducer surface derived from cotton is compared with cotton filter paper, and nanocrystalline cellulose versions of the sensor. X-ray crystallography was employed along with Michaelis-Menten enzyme kinetics, and circular dichroism to contrast the structure/function relations of the peptide-cellulose conjugate conformation to enzyme/substrate binding and turnover rates. The nanocellulosic aerogel was found to have a cellulose II structure. The spatiotemporal relation of crystallite surface to peptide-cellulose conformation is discussed in light of observed enzyme kinetics. A higher substrate binding affinity (K-m) of elastase was observed with the nanocellulose aerogel and nanocrystalline peptide-cellulose conjugates than with the solution-based elastase substrate. An increased K-m observed for the nanocellulosic aerogel sensor yields a higher enzyme efficiency (k(cat)/K-m), attributable to binding of the serine protease to the negatively charged cellulose surface. The effect of crystallite size and beta-turn peptide conformation are related to the peptide-cellulose kinetics. Models demonstrating the orientation of cellulose to peptide O6-hydroxymethyl rotamers of the conjugates at the surface of the cellulose crystal suggest the relative accessibility of the peptide-cellulose conjugates for enzyme active site binding.
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