Catalysis in peptide synthesis

Bodanszky, Miklos

doi:10.1007/bf01025369

Cited by 17 publications

(13 citation statements)

References 85 publications

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“…Peptide synthesis was performed manually using tBOC chemistry [79][80][81][82][83] (Synthetic Proteomics, Carlsbad, CA) or in an automated instrument using FMOC chemistry [81][82][83][84] (Peptide Core Facility in the School of Medicine of the University of North Carolina at Chapel Hill, Chapel Hill, North Carolina). Selection of synthetic method to synthesize the peptides was based on the techniques used by the specific facility.…”

Section: Peptide Synthesismentioning

confidence: 99%

Novel antimicrobial peptides that exhibit activity against select agents and other drug resistant bacteria

Venugopal¹,

Klapper²,

Srouji³

et al. 2010

Bioorganic & Medicinal Chemistry

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Section: Peptide Synthesismentioning

confidence: 99%

Novel antimicrobial peptides that exhibit activity against select agents and other drug resistant bacteria

Venugopal¹,

Klapper²,

Srouji³

et al. 2010

Bioorganic & Medicinal Chemistry

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“…The procedure described for cyclization in ref. (29) was closely followed. From 0.50 g protected pentapeptide hydrazide 0.20 g (55%) cyclopentapeptide, m.p.…”

Section: Cyclo-d -Alanyl-d-alanyl-l-isoleucyl-d-leucyl-l -mentioning

confidence: 99%

Allomalformin†

Bodanszky

Bednarek

Yiotakis

et al. 1982

International Journal of Peptide and Protein Research

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In an attempt to find explanation for the initial erroneous sequence assignment for malformin, a sequence‐isomer of the natural product, 3‐isoleucine‐5‐valine malformin or briefly “allomalformin” that on partial acid hydrolysis could have given rise to misleading fragments, was synthesized and compared with both natural and synthetic preparations of malformin. Allomalformin is identical to the parent microbial peptide (malformin A, or briefly malformin) with respect to biological activity and conformation (ORD and CD spectra) and is indistinguishable from it by high pressure liquid chromatography. Yet, the two isomers have slightly different Rf values on thin‐layer chromatograms and by this method no allomalformin could be detected in samples of the natural product. On the other hand both high pressure liquid chromatography and thin‐layer chromatography demonstrated the presence of the lower homolog, 5‐valine malformin, in the samples examined. On partial acid hydrolysis this natural analog should liberate Val‐Cys, while Cys‐Val forms from malformin itself. Similarly, the corresponding desthio cyclopentapeptides should give rise to Val‐Ala and Ala‐Val respectively; the former being more resistant to further hydrolysis persists in the partial hydrolysates. The presence of Val‐Cys in partial hydrolysates of malformin and of Val‐Ala in the partial hydrolysates of desthiomalformin, both originating from the accompanying lower homolog rather than from malformin itself, is likely to have led to the postulation of the erroneous Cys‐Val‐Cys partial sequence.

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“…0.44,Rf4 0.58. (1 2) (13). The above dipeptide ester in MeOH was treated with hydrazine hydrate and the product was purified by precipitation from MeOH with ether, followed by column chromatography on silica- ( 14).…”

Section: Z( 0me)-tyr-ile-a Sn-leu-ile-thr-a Rg(mts)-gln-arg(mts)-tyr-nhzmentioning

confidence: 99%

“…Lys(Z), Glu(OBz1) and Arg(Mts) (10). In addition, we employed Asp(0Chp) (1 l), adjacent to Asn, Ala and Leu, in order to suppress base-catalyzed succinimide formation (12)(13)(14). This protecting group is stable to TFA, but smoothly cleaved by the above mentioned acidic reagent.…”

mentioning

confidence: 99%

Synthesis of porcine neuropeptide Y(NPY) in solution

Kiyama

Ooi

Kitagawa

et al. 1987

International Journal of Peptide and Protein Research

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The porcine neuropeptide Y (NPY), a 36‐residue peptide amide, was synthesized by assembling six peptide fragments followed by thioanisole‐mediated deprotection with trifluoromethanesulfonic acid in trifluoroacetic acid. β‐Cycloheptyl aspartate, Asp(OChp), was employed to suppress base‐catalyzed succinimide formation. When administered to dogs, the purified peptide (10μg/kg) caused prolonged increase of systemic arterial blood pressure and decreased pancreatic blood flow.

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Catalysis in peptide synthesis

Cited by 17 publications

References 85 publications

Novel antimicrobial peptides that exhibit activity against select agents and other drug resistant bacteria

Novel antimicrobial peptides that exhibit activity against select agents and other drug resistant bacteria

Allomalformin†

Synthesis of porcine neuropeptide Y(NPY) in solution

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