Fluorinated Aromatic Amino Acids Distinguish Cation-π Interactions from Membrane Insertion
نویسندگان
چکیده
منابع مشابه
Fluorinated Aromatic Amino Acids Distinguish Cation-π Interactions from Membrane Insertion.
Cation-π interactions, where protein aromatic residues supply π systems while a positive-charged portion of phospholipid head groups are the cations, have been suggested as important binding modes for peripheral membrane proteins. However, aromatic amino acids can also insert into membranes and hydrophobically interact with lipid tails. Heretofore there has been no facile way to differentiate t...
متن کاملAromatic Amino Acids-Guanidinium Complexes through Cation-π Interactions.
Continuing with our interest in the guanidinium group and the different interactions than can establish, we have carried out a theoretical study of the complexes formed by this cation and the aromatic amino acids (phenylalanine, histidine, tryptophan and tyrosine) using DFT methods and PCM-water solvation. Both hydrogen bonds and cation-π interactions have been found upon complexation. These in...
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The cation-pi interaction is a general, strong, noncovalent binding force that is used throughout nature. The side chains of the aromatic amino acids [phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp)] provide a surface of negative electrostatic potential than can bind to a wide range of cations through a predominantly electrostatic interaction. In this brief overview, the fundamental n...
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The cation-p interaction is a general, strong, noncovalent binding force that is used throughout nature. The side chains of the aromatic amino acids [phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp)] provide a surface of negative electrostatic potential than can bind to a wide range of cations through a predominantly electrostatic interaction. In this brief overview, the fundamental na...
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Fluorination became the more radical approach for modification of leading compounds in medicinal chemistry [1,2]. Due to its small size and high electronegativity, fluorine forms a strong covalent bond with carbon, shows a significant impact on neighboring groups that alter the stability and reactivity of the molecules, helps to creates more stable protein folds [3,4]. Fluorinated amino acids w...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2015
ISSN: 0021-9258
DOI: 10.1074/jbc.m115.668343