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Investigating Cellulose Binding of Peptides Derived from Carbohydrate Binding Module 1. | LitMetric

AI Article Synopsis

  • Carbohydrate-binding modules (CBMs) are now recognized for their utility in tasks like protein purification and modifying cellulose fibers, requiring attachment to target proteins for effectiveness.
  • Researchers explored whether shorter, less hydrophobic peptides derived from CBMs could effectively bind to nanocrystalline cellulose (NCC) or cotton linter paper as effectively as full-length CBMs.
  • The study found that these designed peptides, despite variations in their structure and hydrophobicity, bound to cellulose with similar affinity as traditional CBMs, suggesting potential for using peptide-conjugates to enhance cellulose-based materials.

Article Abstract

Carbohydrate-binding modules (CBM) have emerged as useful tools for a wide range of tasks, including the use as purification tags or for cellulose fiber modification. For this purpose, the CBM needs to be attached to a target protein leading to large constructs. We investigated if short peptides from the carbohydrate binding site of CBMs can bind in a similar way as native, full-length CBMs to nanocrystalline cellulose (NCC) or cotton linter paper. We designed our cellulose-binding peptides to be less hydrophobic and shorter than those previously reported. Starting from the binding site of Cel7A-CBM1, we incorporated the essential amino acids involved in cellulose binding into our peptides. These peptides, as well as control peptides with scrambled sequences or a lack of essential amino acids, bound to cellulose with similar affinity as CBM regardless of their secondary structure, sequence, or hydrophobicity. This unspecific mode of cellulose binding displayed by the presented peptides may be exploited to functionalize cellulose-based biomaterials by means of peptide-conjugates.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11389687PMC
http://dx.doi.org/10.1021/acs.biomac.4c00575DOI Listing

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