82911-79-3Relevant articles and documents
Aldolase Cascade Facilitated by Self-Assembled Nanotubes from Short Peptide Amphiphiles
Afrose, Syed Pavel,Das, Dibyendu,Reja, Antara
supporting information, p. 4329 - 4334 (2020/02/05)
Early evolution benefited from a complex network of reactions involving multiple C?C bond forming and breaking events that were critical for primitive metabolism. Nature gradually chose highly evolved and complex enzymes such as lyases to efficiently facilitate C?C bond formation and cleavage with remarkable substrate selectivity. Reported here is a lipidated short peptide which accesses a homogenous nanotubular morphology to efficiently catalyze C?C bond cleavage and formation. This system shows morphology-dependent catalytic rates, suggesting the formation of a binding pocket and registered enhancements in the presence of the hydrogen-bond donor tyrosine, which is exploited by extant aldolases. These assemblies showed excellent substrate selectivity and templated the formation of a specific adduct from a pool of possible adducts. The ability to catalyze metabolically relevant cascade transformations suggests the importance of such systems in early evolution.
Synthesis of chlorophyll-amino acid conjugates as models for modification of proteins with chromo/fluorophores
Tamiaki, Hitoshi,Isoda, Yasuaki,Tanaka, Takuya,Machida, Shinnosuke
, p. 1421 - 1428 (2014/03/21)
A chlorophyll-a derivative bonded directly with epoxide at the peripheral position of the chlorin π-system was reacted with N-urethane and C-ester protected amino acids bearing an alcoholic or phenolic hydroxy group as well as a carboxy group at the residue to give chlorophyll-amino acid conjugates. The carboxy residues of N,C-protected aspartic and glutamic acids were esterified with the epoxide in high yields. The synthetic conjugates in dichloromethane had absorption bands throughout the visible region including intense red-side Qy and blue-side Soret bands. By their excitation at the visible bands, strong and efficient fluorescence emission was observed up to the near-infrared region. The chromo/fluorophores are promising for preparation of functional peptides and modification of proteins.
Enzyme promotes the hydrogelation from a hydrophobic small molecule
Gao, Jie,Wang, Huaimin,Wang, Ling,Wang, Jingyu,Kong, Deling,Yang, Zhimou
supporting information; scheme or table, p. 11286 - 11287 (2011/03/19)
(Chemical Equation Presented) We report in this paper that an enzymatic reaction can be used as the sole mechanism for forming supramolecular hydrogels that have good stability in aqueous solutions at room temperature. The gels are two-component hydrogels that are mainly formed by hydrophobic compound 2 and doped with hydrophilic compound 1. They were formed by an enzymatic process that produces hydrophobic 2 in homogeneous modes and assists the formation of three-dimensional networks. We have characterized the morphologies of the gels with scanning electron microscopy and dark-field transmission electron microscopy, collected fluorescence data to monitor the gelation process, and proposed a possible mechanism to explain the formation of the gels.