Example：10.1021/acsami.1c06204 or Chem. Rev., 2007, 107, 2411-2502
Composition‐dependent multivalency of peptide–peptide interactions revealed by tryptophan‐scanning mutagenesis Journal of Peptide Science (IF1.905), Pub Date : 2021-03-03, DOI: 10.1002/psc.3310 Lanlan Yu, Yongfang Zheng, Xiaocui Fang, Yimin Zou, Chenxuan Wang, Yanlian Yang, Chen Wang
We have examined in this contribution the composition dependence of binding characteristics in peptide–peptide interactions between an oligopeptide octa‐glycine and a series of tryptophan‐containing octapeptides. The binding energy associated with tryptophan–glycine interactions manifests pronounced stepwise binding characteristics as the number of tryptophan increases from 0 to 8 in the octapeptides consisting only of glycine and can be attributed to mono‐, di‐, and tri‐valent peptide–peptide interactions. At the same time, only weak fluctuations in binding energy were observed as the number of tryptophan increases from 2 to 7. Such distinctive nonlinearity of composition‐dependent tryptophan–glycine binding energy characteristics due to continuously varying tryptophan compositions in the octapeptides could be considered as a reflection of combinatorial contributions due to the hydrogen bonds originated from the indole moieties of tryptophan with the main chains of octapeptide of glycine containing N–H and C=O moieties and the van der Waals interactions (including π–π and π–CH interactions) between peptides.