455-64-1

Upstream product

• 263843-55-6 Arg-Arg-AMC 
• 79-14-1 glycolic Acid 
• 74-79-3 L-arginine 
• 56-84-8 L-Aspartic acid 
• 15483-59-7 Arg₂-2-naphthylamine 

Relevant academic research and scientific papers

Ester-mediated peptide formation promoted by deep eutectic solvents: a facile pathway to proto-peptides

The ester-amide exchange reaction enables spontaneous formation of prebiotic proto-peptides under mild conditions. However, this reaction also leads to oligomers with a vast sequence diversity of ester and amide linkages. Here, we demonstrate using deep eutectic solvents as a universal strategy to regulate the reaction pathways and promote the formation of amino acid-enriched oligomers with peptide backbones.

Identification and characterization of prokaryotic dipeptidyl-peptidase 5 from porphyromonas gingivalis

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.

Modelling of prebiotic synthesis and selection of peptides under isothermal conditions and thermal cycling mode

The model peptide synthesis from mixtures of amino acids was carried out under the thermal cycling and isothermal modes. The compositions of the obtained mixtures of products and the primary amino acid sequence of the synthesized peptides were determined by Fourier transform ion cyclotron resonance mass spectrometry and tandem mass spectrometry in combination with high-performance liquid chromatography with the application of de novo sequencing of the synthesized products. The processes of abiogenous synthesis of peptides were shown to occur under relatively mild temperature conditions and give a substantially less number of peptides as compared with the possible statistical set. The evolution of the system takes place in the process of the synthesis in solid phase with the disappearance of a series of the most unstable peptides. The selection process with the formation of complementary peptides takes place in peptide synthesis under the thermal cyclic mode.

A novel L-amino acid ligase from Bacillus subtilis NBRC3134, a microorganism producing peptide-antibiotic rhizocticin

L-Amino acid ligase catalyzes the formation of an α-peptide bond from unprotected L-amino acids in an ATP-dependent manner, and this enzyme is very useful in efficient peptide production. We performed enzyme purification to obtain a novel L-amino acid lig

Compositions and Methods for Binding Lysophosphatidic Acid

Compositions and methods for making and using anti-LPA agents, for example, monoclonal antibodies, are described.

Intramolecularly-quenched near infrared fluorescent probes

An intramolecularly-quenched, near infrared fluorescence probe that emits substantial fluorescence only after interaction with a target tissue (i.e., activation) is disclosed. The probe includes a polymeric backbone and a plurality of near infrared fluorochromes covalently linked to the backbone at fluorescence-quenching interaction-permissive positions separable by enzymatic cleavage at fluorescence activation sites. The probe optionally includes protective chains or fluorochrome spacers, or both. Also disclosed are methods of using the intramolecularly-quenched, near infrared fluorescence probes for in vivo optical imaging.

Disulfide bridged cyclic peptides containing a cgridri sequence useful in control of hypertension

Disulfide bridged cyclic peptides are described which are preferably 13 to 20 amino acid residues in length and which include the endocyclic sequence cys-gly-arg-ile-asp-arg-ile. Peptides of this class are selective for and show picomolar-range affinity for the non-guanyl cyclase-coupled atrial peptide receptor. Affinity for this receptor is associated with potentiation of the mean arterial pressure response to atrial peptide and these peptides are therefore useful in control of hypertension. Peptides of most interest are of the formula wherein X1 is the peptidic fragment ser-ser; wherein X2 is a peptidic fragment selected from gly-ser-gly-leu, gly-ala-gly-leu and gly-leu; wherein X3 is the peptidic fragment asn-ser-phe-arg; wherein m is zero or one, n is one and r is one; and wherein A represents an amino terminus or its pharmaceutically--acceptable salt, and B represents a carboxyl terminus or its pharmaceutically-acceptable ester, amide or salt.