通过疏水簇集和组氨酸-芳香族相互作用来确定结构的氨基酸可产生具有生物活性的拟肽。
Amino acids that specify structure through hydrophobic clustering and histidine-aromatic interactions lead to biologically active peptidomimetics.
作者信息
Graciani N R, Tsang K Y, McCutchen S L, Kelly J W
机构信息
Department of Chemistry, Texas A&M University, College Station 77843-3255.
出版信息
Bioorg Med Chem. 1994 Sep;2(9):999-1006. doi: 10.1016/s0968-0896(00)82048-9.
PMID:7712134
Abstract
Acyclic beta-sheet structure can be nucleated in heptapeptides when the 4-(2-aminoethyl)-6-dibenzofuranpropanoic acid residue (1) is flanked in sequence by two His residues, a His residue and a hydrophobic residue or by two hydrophobic residues. Acyclic beta-sheet peptidomimetics having an appropriate sequence have sufficient structural integrity to exhibit antimicrobial activity equivalent to that of gramicidin S.
摘要
当4-(2-氨基乙基)-6-二苯并呋喃丙酸残基(1)在序列上两侧分别为两个组氨酸残基、一个组氨酸残基和一个疏水残基或两个疏水残基时，非环β-折叠结构可在七肽中形成核。具有适当序列的非环β-折叠肽模拟物具有足够的结构完整性，以表现出与短杆菌肽S相当的抗菌活性。
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