64472-24-8

Upstream product

• 41324-66-7 H-Pro-OBzl 
• 29776-78-1 (S)-1-(2-tert-butoxycarbonylaminoacetyl)pyrrolidine-2-carboxylic acid benzyl ester 

Downstream Products

• 112302-77-9 Boc-Leu-Phe-Gly-Pro-NHNH₂ 
• 136314-94-8 cyclo(L-Phe-L-Pro-Gly-L-Pro)2 
• 136236-56-1 Boc-L-Phe-L-Pro-Gly-L-Pro-L-Phe-L-Pro-Gly-L-Pro-OSu 
• 136206-73-0 Boc-L-Phe-L-Pro-Gly-L-Pro-L-Phe-L-Pro-Gly-L-Pro-OBzl 
• 136206-75-2 L-Phe-L-Pro-Gly-L-Pro-L-Phe-L-Pro-Gly-L-Pro-OSu 
• 136206-74-1 Boc-L-Phe-L-Pro-Gly-L-Pro-L-Phe-L-Pro-Gly-L-Pro 
• 136206-71-8 Boc-L-Phe-L-Pro-Gly-L-Pro 
• 136206-72-9 L-Phe-L-Pro-Gly-L-Pro-OBzl 
• 1026191-35-4 Boc-Gly-Pro-Gly-Pro-Phe-Pro-Phe-Pro-OSu 
• 1026053-86-0 Boc-Gly-Pro-Gly-Pro-Phe-Pro-Phe-Pro-OBzl 
• 1026503-27-4 H-Gly-Pro-Gly-Pro-Phe-Pro-Phe-Pro-OSu 
• 149297-00-7 Boc-Gly-Pro-Gly-Pro-Phe-Pro-Phe-Pro-OH 
• 86857-05-8 N-<4-(4-hydroxyphenyl)butyryl>-L-prolyl-DL-α-methyltyrosylglycyl-L-proline benzyl ester 
• 86850-61-5 N-<4-(4-hydroxyphenyl)butyryl>-L-prolyl-DL-α-methylphenylalanylglycyl-L-proline benzyl ester 

Relevant academic research and scientific papers

The Study of Stability of Proline-Containing Derivatives of Dopamine and Serotonin in the Biological Media in Vitro Experiments

Abstract—: The peptides Boc-Gly-Pro-DP, Z-Gly-Pro-DP, LA-Gly-Pro-DP, Boc-Gly-Pro-Srt, Z-Gly-Pro-Srt have been synthesized for the first time. The study of their stability in the presence of leucine aminopeptidase, carboxypeptidase Y, carboxypeptidase B, and proline endopeptidase (PEP) has shown that the synthesized peptides are stable in the presence of aminopeptidases and carboxypeptidases. In the presence of PEP, dopamine (DP) and serotonin (Srt) have been cleaved from these substances. Thus, the originally synthesized proline derivatives of Srt and DP may be considered as the resources, from which Srt and DP can be gradually released. This creates the possibility of a prolonged action of these biologically active compounds on cells and, consequently, on the whole body.

Conformational studies of cyclo(L-Phe-L-Pro-Gly-L-Pro)2 by 1H- and 13C-nuclear magnetic resonance spectroscopy, and its enantioface-differentiating ability

Analyses of the 1H- and 13C-nuclear magnetic resonance (1H- and 13C-NMR) spectra of the cyclooctapeptide cyclo (L-Phe-L-Pro-Gly-L-Pro)2 (3) in CDCl3 with the aid of the C-H correlated spectroscopy (C-H COSY) two-dimensional NMR spectrum (Fig. 2) suggested that two kinds of C2-symmetric conformation with all trans and cis-trans-trans-trans forms coexist. When 0.5 eq of CsSCN or 1 eq of D- and L-PheOMe · HCl (D/L ratio = 1/2) was added to a solution of the cyclooctapeptide (3) in CDCl3, the 1H- and 13C-NMR spectra (Fig. 3) suggested the presence of only one C2-symmetric conformation (all trans), resulting from the formation of complexes with CsSCN or D- and L-PheOMe · HCl. The 13C-NMR spectra of the complexes of the cyclooctapeptide (3 or 4) with D- and L-PheOMe · HCl displayed separate resonances for each carbon atom of D-PheOMe · HCl and L-PheOMe · HCl. Furthermore, the ability of 3 to distinguish the D from the L enantiomer, is superior to that of 4 (Table II).

Conformational studies of cyclo(L-Phe-L-Pro-Gly-L-Pro)2 by 13C nuclear magnetic resonance

The 13C-NMR spectrum of cyclooctapeptide cyclo(L-PHe-L-Pro-Gly-L-Pro)2 (A) in CDCl3 suggested that its conformation involved the coexistence of two kinds of C2-symmetric conformation with trans-trans-trans-trans

The L-Proline Residue as a 'Break-point' in Metal - Peptide Systems

Results are reported of a potentiometric and spectrophotometric study of the H+ and Cu2+ complexes of the tetrapeptides X-Gly-Gly-Gly, Gly-X-Gly-Gly, Gly-Gly-X-Gly, and Gly-Gly-Gly-X where X is the proline (Pro) and sarcosine (Sar) residue (Gly=glycine).All the tetrapeptides (HL) form the series of complexes , -1L>, -2L>, and -3L> (charges omitted).The ligands Gly-X-Gly-Gly also form the bis-complex, .When inserted in a peptide chain the Pro and Sar residues cannot co-ordinate to Cu2+ through their peptide nitrogens since they do not possess ionizable protons.In addition the Pro residue tends to force the peptide chain to form a 'β-turn' and so adopt a 'bent' conformation.These studies demonstrate the formation of a large chelate ring when tetrapeptides containing Pro (and , to a smaller extent, Sar) in the second or third positions co-ordinate to Cu2+.This ring spans the terminal residues of the peptide chain and locks the peptide into a 'bent' or 'horse-shoe' shaped conformation.Cu2+ could therefore play an important role in activating oligopeptides (e.g. neuropeptides) containing proline.

Renally active tetrapeptides

N-Acyltetrapeptides are described which are active in improving renal function. An exemplary species is N-4-(4-hydroxyphenyl)-butyryl-L-prolyl-D,L-α-methylphenylalanyl-glycyl-L-proline.