37682-75-0Relevant academic research and scientific papers
N-Carboxyanhydride-Mediated Fatty Acylation of Amino Acids and Peptides for Functionalization of Protocell Membranes
Izgu, Enver Cagri,Bj?rkbom, Anders,Kamat, Neha P.,Lelyveld, Victor S.,Zhang, Weicheng,Jia, Tony Z.,Szostak, Jack W.
supporting information, p. 16669 - 16676 (2017/01/10)
Early protocells are likely to have arisen from the self-assembly of RNA, peptide, and lipid molecules that were generated and concentrated within geologically favorable environments on the early Earth. The reactivity of these components in a prebiotic environment that supplied sources of chemical energy could have produced additional species with properties favorable to the emergence of protocells. The geochemically plausible activation of amino acids by carbonyl sulfide has been shown to generate short peptides via the formation of cyclic amino acid N-carboxyanhydrides (NCAs). Here, we show that the polymerization of valine-NCA in the presence of fatty acids yields acylated amino acids and peptides via a mixed anhydride intermediate. Notably, Nα-oleoylarginine, a product of the reaction between arginine and oleic acid in the presence of valine-NCA, partitions spontaneously into vesicle membranes and mediates the association of RNA with the vesicles. Our results suggest a potential mechanism by which activated amino acids could diversify the chemical functionality of fatty acid membranes and colocalize RNA with vesicles during the formation of early protocells.
Identification and characterization of prokaryotic dipeptidyl-peptidase 5 from porphyromonas gingivalis
Ohara-Nemoto, Yuko,Rouf, Shakh M. A.,Naito, Mariko,Yanase, Amie,Tetsuo, Fumi,Ono, Toshio,Kobayakawa, Takeshi,Shimoyama, Yu,Kimura, Shigenobu,Nakayama, Koji,Saiki, Keitarou,Konishi, Kiyoshi,Nemoto, Takayuki K.
, p. 5436 - 5448 (2014/03/21)
Porphyromonas gingivalis, a Gram-negative asaccharolytic anaerobe, is a major causative organism of chronic periodontitis. Because the bacterium utilizes amino acids as energy and carbon sources and incorporates them mainly as dipeptides, a wide variety of dipeptide production processes mediated by dipeptidyl-peptidases (DPPs) should be beneficial for the organism. In the present study, we identified the fourth P. gingivalis enzyme, DPP5. In a dpp4-7-11-disrupted P. gingivalis ATCC 33277, a DPP7-like activity still remained. PGN-0756 possessed an activity indistinguishable from that of the mutant, and was identified as a bacterial orthologue of fungal DPP5, because of its substrate specificity and 28.5% amino acid sequence identity with an Aspergillus fumigatus entity. P. gingivalis DPP5 was composed of 684 amino acids with a molecular mass of 77,453, and existed as a dimer while migrating at 66 kDa on SDS-PAGE. It preferred Ala and hydrophobic residues, had no activity toward Pro at the P1 position, and no preference for hydrophobic P2 residues, showed an optimal pH of 6.7 in the presence of NaCl, demonstrated Km and kcat/Km values for Lys-Ala-MCA of 688 μM and 11.02 μM-1 s-1, respectively, and was localized in the periplasm. DPP5 elaborately complemented DPP7 in liberation of dipeptides with hydrophobic P1 residues. Examinations of DPP- and gingipain gene-disrupted mutants indicated that DPP4, DPP5, DPP7, and DPP11 together with Arg- and Lys-gingipains cooperatively liberate most dipeptides from nutrient oligopeptides. This is the first study to report that DPP5 is expressed not only in eukaryotes, but also widely distributed in bacteria and archaea.
Amino Acids and Peptides. Part 32. Total Synthesis of Eglin c. Part 2. Synthesis of a Heptacontapeptide corresponding to the Entire Amino Acid Sequence of Eglin c and of Related Peptides, and Studies on the Relationship between the Structure and Inhibitor
Okada, Yoshio,Tsuboi, Satoshi
, p. 3321 - 3328 (2007/10/02)
Commencing with a protected C-terminal triacontapeptide of eglin c, eglin c (31-70), eglin c (22-30) and eglin c (8-70) and finally eglin c were synthesized by a conventional solution method in order to allow us to study the relationship between their str
SYNTHESIS OF DINITROPHENYLTETRAPEPTIDES AS CHROMOPHORIC SUBSTRATES OF ENDOPROTEINASES
Kulikov, S. V.,Sokolova, N. Yu.,Rodin, S. V.,Samartsev, M. A.
, p. 469 - 475 (2007/10/02)
The synthesis has been performed of ten tetrapeptides of the general formula Dnp-Gly-Gly-X-Arg-OH, where X = Val, Phe, Abu, Asp(OBut), Asp, Met, D-Phe, Ser, Thr, or Trp.The synthesis was carried out with Dnp-Gly-Gly-Onp, activated esters of pro
