658-79-7Relevant articles and documents
Novel peptide with a specific calcium-binding capacity from whey protein hydrolysate and the possible chelating mode
Zhao, Lina,Huang, Qimin,Huang, Shunli,Lin, Jiaping,Wang, Shaoyun,Huang, Yifan,Hong, Jing,Rao, Pingfan
, p. 10274 - 10282 (2014)
A novel peptide with a specific calcium-binding capacity was isolated from whey protein hydrolysates. The isolation procedures included diethylaminoethyl (DEAE) anion-exchange chromatography, Sephadex G-25 gel filtration, and reversed-phase high-performance liquid chromatography (HPLC). A peptide with a molecular mass of 237.99 Da was identified by liquid chromatography-electrospray ionization/mass spectrometry (LC-ESI/MS), and its amino acid sequence was confirmed to be Gly-Tyr. The calcium-binding capacity of Gly-Tyr reached 75.38 μg/mg, increasing by 122% when compared to the hydrolysate complex. The chelating interaction mode between the Gly-Tyr and calcium ion was investigated, indicating that the major binding sites included the oxygen atom of the carbonyl group and nitrogen of the amino or imino group. The folding and structural modification of the peptide arose along with the addition of the calcium ion. The profile of 1H nuclear magnetic resonance (NMR) spectroscopy demonstrated that the electron cloud density around the hydrogen nucleus in the peptide changed was caused by the calcium ion. The results of ζ potential showed that the Gly-Tyr-Ca chelate was a neutral molecule in which the calcium ion was surrounded by the specific binding sites of the peptide. Moreover, thermogravimetry-differential scanning calorimetry (TG-DSC) and calcium-releasing assay revealed that the Gly-Tyr-Ca chelate exerted excellent thermal stability and solubility in both acidic and basic conditions, which were beneficial to calcium absorption in the gastrointestinal tract of the human body and, therefore, improved its bioavailability. These findings further the progress in the research of whey protein, suggesting the potential in making peptide-calcium chelate as a dietary supplement.
Identification of novel L-amino acid α-ligases through hidden markov model-based profile analysis
Senoo, Akihiro,Tabata, Kazuhiko,Yonetani, Yoshiyuki,Yagasaki, Makoto
body text, p. 415 - 418 (2010/09/30)
L-Amino acid α-ligase (Lal), catalyzing the formation of α-dipeptides from unprotected l-amino acids in an ATP-dependent manner, is used in cost-effective fermentative production of dipeptides. We searched for novel Lals by in silico screening using Hidden Markov Model-based profile analysis, and identified five novel Lals that showed low similarity and different substrate specificity from known Lals.
Increased stability of peptidesulfonamide peptidomimetics towards protease catalyzed degradation
De Bont, Dries B.A.,Sliedregt-Bol, Karen M.,Hofmeyer, Lovina J. F.,Liskamp, Rob M. J.
, p. 1043 - 1047 (2007/10/03)
Replacement of amide bonds in peptides by sulfonamide moieties resulted in peptidosulfonamides with an increased stability towards protease catalyzed degradation. In addition to protection of the protease cleavage site, it was found that introduction of a sulfonamide also influenced the stability of adjacent amide bonds. Copyright (C) 1999 Elsevier Science Ltd.
