Reductive Cleavage of Acylproline Peptide Bonds<sup>*</sup>

Wf, Benisek; Ma, Raftery; Rd, Cole

doi:10.1021/bi00864a023

Cited by 45 publications

(14 citation statements)

References 21 publications

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“…Amino acid analysis of this material, which represented about 70% of the product, indicated the loss of threonine, proline, lysine and alanine from the B-chain S-sulpho derivative and suggested that the majority of the material had undergone reductive cleavage at the secondary amide bond between threonine-27 and proline-28 of the B-chain. The extent of cleavage was about the same as that found previously (Benisek et al, 1967;Katsoyannis et al, 1971a), even though the earlier workers exposed the peptide to sodium for a longer time.…”

Section: Resultssupporting

confidence: 82%

“…Cleavage of acyl proline bonds in this way is, of course, well documented in the literature (see, e.g., Benisek et al, 1967) and the reaction has, in fact, been exploited in synthesis. Katsoyannis et al (1971a) have shown that the truncated B-chain can be recombined with Achain to give an analogue of insulin which possessed biological activity similar to that of insulin itself.…”

Section: Discussionmentioning

confidence: 89%

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2-Sulphobenzyl, a new solubilizing and reversible protecting group for cysteine in proteins. Its scope and limitations

Rüegg¹,

Jarvis²,

Rudinger³

1979

Biochemical Journal

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S-2-Sulphobenzylcysteine and S-2-(sulphomethyl)benzylcysteine are prepared by alkylation of cysteine with omega-toluenesultone and 2,3-benzo-1,4-butanesultone respectively. Owing to the presence of the sulphonic acid group, these protected cysteine derivatives are extremely water-soluble and are stable to acid hydrolysis. The groups can be removed by treatment with sodium in liquid NH3. Reduction with tributylphosphine and simultaneous alkylation of insulin with toluenesultone under mild conditions (pH 8.3, aq. 50% propanol) gives the fully S-substituted derivatives in excellent yield; they can be separated by isoelectric precipitation of the S-sulphobenzylated B-chain. Treatment of the latter with sodium in liquid NH3 led simultaneously to the removal of the protecting groups and to the well-documented cleavage at the threonine-proline bond which can be prevented by addition of sodium amide. When deprotected A-chain was recombined with B-chain, insulin was isolated in the same yield and with the same degree of biological activity as that in the control experiment.

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Section: Resultssupporting

confidence: 82%

Section: Discussionmentioning

confidence: 89%

2-Sulphobenzyl, a new solubilizing and reversible protecting group for cysteine in proteins. Its scope and limitations

Rüegg¹,

Jarvis²,

Rudinger³

1979

Biochemical Journal

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“…These compounds can be explained as reaction intermediates still containing the asparagine but with a hydroxyl group at either C1 or C4. C1 reduction would lead to 2‐amino,3‐glyco‐carbamoyl‐propanol reminiscent of the chemical mechanism of reductive alkaline cleavage of peptide bonds . Reduction at C4, however, appears even more likely than at C1 as the product of reductive chemical cleavage was reported to have an hydroxyl group at C4 of the former Asn .…”

Section: Resultsmentioning

confidence: 99%

Reductive Alkaline Release of N‐Glycans Generates a Variety of Unexpected, Useful Products

Figl

Altmann

2018

Proteomics

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Release of O-glycans by reductive β-elimination has become routine in many glyco-analytical laboratories and concomitant release of N-glycans has repeatedly been observed. Revisiting this somewhat forgotten mode of N-glycan release revealed that all kinds of N-glycans including oligomannosidic and complex-type N-glycans from plants with 3-linked fucose and from mammals with or without 6-linked fucose and with sialic acid could be recovered. However, the mass spectra of the obtained products revealed very surprising facts. Even after 16 h incubation in 1 M sodium borohydride, a large part of the glycans occurred in reducing form. Moreover, about one third emerged in the form of the stable amino-functionalized 1-amino-1-deoxy-glycitol. When avoiding acidic conditions, considerable amounts of glycosylamine were observed. In addition, a compound with a reduced asparagine and de-N-acetylation products, in particular of sialylated glycans, was seen. The relative yields of the products reducing glycosylamine, reducing N-glycan, 1-amino-1-deoxy-glycitol or glycitol could be controlled by the release conditions, foremost by temperature and borohydride concentration. Thus, chemical release of N-glycans constitutes a cost-saving alternative to enzymatic hydrolysis for the preparation of precursors for the production of reference compounds for various formats of N-glycan analysis. Moreover, it allows to obtain a stable amino-functionalized glycan derivative, which can be employed to construct glycan arrays or affinity matrices.

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“…The spots were detected by chlorination followed by 1% Optical rotations were measured with a Carl Zeiss Polarimeter (0.001'). For amino acid analysis (1 1) the analogs were hydrolyzed for 22 h with 6 N HC1/0.3% phenol (12) in vacuo at 110' and analyzed on a Beckman 121C amino acid analyzer. For the desamino compounds performic acid oxidation was carried out prior to hydrolysis and amino acid analysis (13).…”

Section: Methodsmentioning

confidence: 99%

Antidiuretic and pressor activities of vasopressin analogs with L‐alaninamide and D‐alaninamide substitutions at position 9

Buku

Gazis

Schwartz

1984

International Journal of Peptide and Protein Research

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Analogs of arginine vasopressin (AVP) and lysine vasopressin (LVP) — with an L‐alaninamide residue or a D‐alaninamide residue replacing the naturally occurring glycinamide in position 9 — lose virtually all pressor activity but retain from 10 to 70% of the antidiuretic activity of their parent hormones. These findings, in conjunction with the data of others on the biological consequences of alterations in positions 7 and 8, show that the antidiuretic receptor will tolerate considerably more structural alteration in the C‐terminal tripeptide “tail” of the vasopressins than will the pressor receptor.

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Reductive Cleavage of Acylproline Peptide Bonds^*

Cited by 45 publications

References 21 publications

2-Sulphobenzyl, a new solubilizing and reversible protecting group for cysteine in proteins. Its scope and limitations

2-Sulphobenzyl, a new solubilizing and reversible protecting group for cysteine in proteins. Its scope and limitations

Reductive Alkaline Release of N‐Glycans Generates a Variety of Unexpected, Useful Products

Antidiuretic and pressor activities of vasopressin analogs with L‐alaninamide and D‐alaninamide substitutions at position 9

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Reductive Cleavage of Acylproline Peptide Bonds*

Cited by 45 publications

References 21 publications

2-Sulphobenzyl, a new solubilizing and reversible protecting group for cysteine in proteins. Its scope and limitations

2-Sulphobenzyl, a new solubilizing and reversible protecting group for cysteine in proteins. Its scope and limitations

Reductive Alkaline Release of N‐Glycans Generates a Variety of Unexpected, Useful Products

Antidiuretic and pressor activities of vasopressin analogs with L‐alaninamide and D‐alaninamide substitutions at position 9

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Product

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About

Reductive Cleavage of Acylproline Peptide Bonds^*