20367-99-1Relevant articles and documents
Ultrafast Photoinduced Electron Transfer in Green Fluorescent Protein Bearing a Genetically Encoded Electron Acceptor
Lv, Xiaoxuan,Yu, Yang,Zhou, Meng,Hu, Cheng,Gao, Feng,Li, Jiasong,Liu, Xiaohong,Deng, Kai,Zheng, Peng,Gong, Weimin,Xia, Andong,Wang, Jiangyun
, p. 7270 - 7273 (2015)
Electron transfer (ET) is widely used for driving the processes that underlie the chemistry of life. However, our abilities to probe electron transfer mechanisms in proteins and design redox enzymes are limited, due to the lack of methods to site-specific
Towards a universal organocatalyst for the synthesis of enantioenriched phenylalanine derivatives by enantioselective decarboxylative protonation
Pigeaux, Morgane,Laporte, Romain,Harrowven, David C.,Baudoux, Jér?me,Rouden, Jacques
supporting information, p. 4599 - 4603 (2016/09/23)
Access to enantioenriched non-proteogenic phenylalanine derivatives is described using the enantioselective decarboxylative protonation reaction of amidohemimalonate esters catalysed by various cinchona-based compounds. This study compares the catalytic efficiency as well as the enantioselectivity induced by three types of common organocatalysts, namely thioureas, squaramides and bis-cinchona squaramides. One of the main outcome of this work is the observation of a significant influence of the N-protecting group of the hemimalonate on its interaction with the catalyst. This methodology carried out under mild conditions exhibits good substrate scope and functional group tolerance. A substoichiometric amount of catalyst can also be used in certain cases while affording good yields and selectivities.
Quantitative insight into the design of compounds recognized by the L-type amino acid transporter 1 (LAT1)
Ylikangas, Henna,Malmioja, Kalle,Peura, Lauri,Gynther, Mikko,Nwachukwu, Emmanuel O.,Lepp?nen, Jukka,Laine, Krista,Rautio, Jarkko,Lahtela-Kakkonen, Maija,Huttunen, Kristiina M.,Poso, Antti
supporting information, p. 2699 - 2707 (2015/02/02)
L-Type amino acid transporter 1 (LAT1) is a transmembrane protein expressed abundantly at the blood-brain barrier (BBB), where it ensures the transport of hydrophobic acids from the blood to the brain. Due to its unique substrate specificity and high expression at the BBB, LAT1 is an intriguing target for carrier- mediated transport of drugs into the brain. In this study, a comparative molecular field analysis (CoMFA) model with considerable statistical quality (Q2=0.53, R2=0.75, Q2 SE=0.77, R2 SE=0.57) and good external predictivity (CCC=0.91) was generated. The model was used to guide the synthesis of eight new prodrugs whose affinity for LAT1 was tested by using an in situ rat brain perfusion technique. This resulted in the creation of a novel LAT1 prodrug with l-tryptophan as the promoiety; it also provided a better understanding of the molecular features of LAT1-targeted high-affinity prodrugs, as well as their promoiety and parent drug. The results obtained will be beneficial in the rational design of novel LAT1-binding prodrugs and other compounds that bind to LAT1.
BIOSYNTHETICALLY GENERATED PYRROLINE-CARBOXY-LYSINE AND SITE SPECIFIC PROTEIN MODIFICATIONS VIA CHEMICAL DERIVATIZATION OF PYRROLINE-CARBOXY-LYSINE AND PYRROLYSINE RESIDUES
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Page/Page column 177, (2010/05/13)
Disclosed herein is pyrroline-carboxy-lysine (PCL), a pyrrolysine analogue, which is a natural, biosynthetically generated amino acid, and methods for biosynthetically generating PCL. Also disclosed herein are proteins, polypeptides and peptides that have PCL incorporated therein and methods for incorporating PCL into such proteins, polypeptides and peptides. Also disclosed herein is the site-specific derivatization of proteins, polypeptides and peptides having PCL or pyrrolysine incorporated therein. Also disclosed herein is the crosslinking of proteins, polypeptides and peptides having PCL or pyrrolysine incorporated therein.
Chemoenzymatic synthesis of enantiomerically pure 4-fluoro-3-nitro and 3-fluoro-4-nitro phenylallanine
Vergne, Caroline,Bois-Choussy, Michele,Ouazzani, Jamal,Beugelmans, Rene,,Zhu, Jieping
, p. 391 - 398 (2007/10/03)
Both antipodes of enantiomerically pure 4-fluoro-3-nitrophenylalanine and 3-fluoro-4-nitrophenylalanine were obtained from their corresponding racemates via enzymatic resolution.