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Molecular Recognition: Multipoint Hydrogen Bonding‐Based Molecular Recognition of Amino Acids and Peptide Derivatives in a Porous Metal‐Macrocycle Framework: Residue‐Specificity, Diastereoselectivity, and Conformational Control (Small 22/2021)
Author(s) -
Tashiro Shohei,
Nakata Kosuke,
Hayashi Ryunosuke,
Shionoya Mitsuhiko
Publication year - 2021
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.202170107
Subject(s) - hydrogen bond , residue (chemistry) , peptide , molecular recognition , amino acid , amino acid residue , chemistry , metal , serine , adsorption , stereochemistry , crystal structure , peptide sequence , combinatorial chemistry , molecule , crystallography , organic chemistry , biochemistry , enzyme , gene
In article number 2005803, Shohei Tashiro, Mitsuhiko Shionoya, and co‐workers report residue‐specific recognition of amino acids and peptide derivatives in a porous metal‐macrocycle framework. Among several amino acid residues, serine moieties are site‐ and diastereo‐selectively adsorbed to a certain binding site on the pore surface through multipoint hydrogen bonding as clearly visualized by single‐crystal X‐ray diffraction analysis.