64471-98-3

Upstream product

• 15761-39-4 1-(tert-butoxycarbonyl)-L-proline 
• 1738-68-7 Gly-OBz 
• 3392-10-7 tert-butoxycarbonyl-L-proline N-hydroxysuccinimide ester 
• 1738-76-7 glycine benzyl ester p-toluenesulfonic acid salt 
• 2462-31-9 benzyl 2-aminoacetate hydrochloride 
• 31953-80-7 N-tert-butyloxycarbonyl-(2S)-prolyl-glycine benzyl ester 

Downstream Products

• 55301-13-8 Boc-Gly-Pro-Gly-OBzl 
• 83280-18-6 BOC-phenylalanylprolylglycine benzyl ester 
• 901138-97-4 N-9-fuorenylmethoxycarbonyl-(2S,4R)-4-methylprolyl-(2S)-prolyl-glycine benzyl ester 
• 874306-06-6 (2-{[(S)-1-(2-{2-[2-(2-Dipropylcarbamoylmethoxy-acetylamino)-acetylamino]-acetylamino}-acetyl)-pyrrolidine-2-carbonyl]-amino}-acetylamino)-acetic acid benzyl ester 
• 72122-63-5 bovine β-casomorphin-5 
• 83280-19-7 phenylalanylprolylglycine benzyl ester hydrochloride 
• 103725-70-8 BOC-prolylphenylalanylprolylglycine benzyl ester 
• 115901-40-1 Z-O-benzyltyrosylprolylphenylalanylprolylglycine benzyl ester 
• 80463-63-4 H-Gly-Pro-Gly-OBzl hydrochloride 
• 80451-92-9 Boc-Leu-Gly-Gly-Gly-Pro-Gly-OBzl 
• 1239474-25-9 N-(9-fluorenylmethoxycarbonyl)-(2S,4S)-4-methoxyprolyl-(2S)-prolylglycine benzyl ester 
• 1239474-22-6 N-(9-fluorenylmethoxycarbonyl)-(2S,4S)-4-tert-butoxyprolyl-(2S)-prolylglycine benzyl ester 
• 3705-27-9 (S)-hexahydropyrrolo[1,2-a]pyrazine-1,4-dione 

Relevant academic research and scientific papers

Synthesis and evaluation of in Vivo anti-hypothermic effect of the N- And C-terminus modified thyrotropin-releasing hormone mimetic: [(4S,5S)-(5-methyl-2-oxooxazolidine-4-yl)-carbonyl]-[3-(thiazol-4-yl)-L-alanyl]-L-prolinamide

We explored orally effective thyrotropin-releasing hormone (TRH) mimetics, which show high central nervous system effects in structure–activity relationship studies based on in vivo antagonistic activity on reserpine-induced hypothermia (anti-hypothermic effect) in mice starting from TRH. This led us to the TRH mimetic: [(4S,5S)-(5-methyl-2-oxooxazolidine-4-yl)carbonyl]-[3-(thiazol-4-yl)-L-alanyl]-L-prolinamide 1, which shows a higher anti-hypothermic effect compared with that of TRH after oral administration. We next attempted further chemical modification of the N- and C-terminus of 1 to find more orally effective TRH mimetics. As a result, we obtained several N- and C-terminus modified TRH mimetics which showed high anti-hypothermic effects.

Molecular capture and conformational change of diketopiperazines containing proline residues by epigallocatechin-3-O-gallate in water

The addition of an aqueous solution of diketopiperazine cyclo(Pro-Xxx) (Xxx: amino acid residue) to an aqueous solution of (?)-epigallocatechin-3-O-gallate (EGCg) led to precipitation of the complex of EGCg and cyclo(Pro-Xxx). The molecular capture abilities of cyclo(Pro-Xxx) using EGCg were evaluated by the ratio of the amount of cyclo(Pro-Xxx) included in the precipitates of the complex with EGCg to that of the total cyclo(Pro-Xxx) used. Stronger hydrophobicity of the side chain of the amino acid residue of cyclo(Pro-Xxx) led to a higher molecular capture ability. Furthermore, the molecular capture ability decreased when the side chain of the amino acid residue had a hydrophilic hydroxyl group. When diketopiperazine cyclo(Pro-Xxx), excluding cyclo(D-Pro-L-Ala), was taken into the hydrophobic space formed by the three aromatic A, B, and B′ rings of EGCg, and formed a complex, their conformation was maintained in the hydrophobic space. Based on nuclear Overhauser effect (NOE) measurement, the 3-position methyl group of cyclo(D-Pro-L-Ala) in D2O was axial, whereas that of cyclo(L-Pro-L-Ala) was equatorial. When cyclo(D-Pro-L-Ala) was taken into the hydrophobic space of EGCg and formed a 2:2 complex, its 3-position methyl group changed from the axial position to the equatorial position due to steric hindrance by EGCg.

Collagen mimics

Novel collagen mimics are disclosed with a tripeptide unit having the formula (Xaa-Yaa-Gly)n, where one of the positions Xaa or Yaa is a bulky, non-electron withdrawing proline derivative. By substituting a proline derivative at either the Xaa or Yaa position in the native collagen helix, the stability of the helix is increased due solely to steric effects relative to prior known collagen-related triple helices. Methods are also disclosed for making the novel collagen mimics.

Cation dependence of chloride ion complexation by open-chained receptor molecules in chloroform solution

Seventeen peptides, most having the sequence GGGPGGG, but differing in the C- and N-terminal ends, have been studied as anion-complexing agents. These relatively simple, open-chained peptide systems interact with both chloride and the associated cation. Changes in the N- and C-terminal side chains appear to make little difference in the efficacy of binding. NMR studies suggest that the primary interactions involve amide NH contacts with the chloride anion, and CD spectral analyses suggest a concomitant conformational change upon binding. Changes in binding constants, which are expected in different solvents, also suggest selective solvent interactions with the unbound host that helps to preorganize the open-chained peptide system. Significant differences are apparent in complexation strengths when the heptapeptide chain is shortened or lengthened or when the relative position of proline within the heptapeptide is varied.

SYNTHESIS AND FAST-ATOM BOMBARDMENT MASS SPECTROMETRY OF β-CASOMORPHIN-5

A fully detailed solution synthesis of β-casomorphin-5 (Tyr-Pro-Phe-Pro-Gly) and positive FAB mass spectra of all synthetic intermediates are reported, together with the B/E daughter ion spectrum of the peptide, and the corresponding sequence determination.