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.