Synthesis of two sequential polypeptides by dispersion in benzene and their circular dichroism spectra in aqueous solution: Poly(<scp>L</scp>‐Glu‐<scp>L</scp>‐Lys‐<scp>L</scp>‐Ala‐Gly) and Poly(<scp>L</scp>‐Ala‐<scp>D</scp>‐Glu‐<scp>L</scp>‐Lys‐<scp>D</scp>‐Ala‐Gly)

Zeiger, Allen R.; Lange, Armand; Maurer, Paul H.

doi:10.1002/bip.1973.360120917

Cited by 16 publications

(6 citation statements)

References 19 publications

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“…Ala-Gly-OEt Hydrochloride (2) . Boc-Ala-Gly-OEt ( 1 ), which was prepared as an oil according to the earlier article, was converted to compound 2 by treatment with HCl/dioxane: mp 152 °C; [α] D = 16.7° (lit. 152−154 °C; [α] D = 7.04°, c = 1 in methanol).…”

Section: Methodsmentioning

confidence: 99%

Synthesis and Wettability Characteristics of Model Adhesive Protein Sequences Inspired by a Marine Mussel

2000

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Three adhesive polyoctapeptides (X/Y-Gly-Tyr-Ser-Ala-Gly-Tyr-Lys)n (X, Thr and Ala: Y, Thr:Ala = 3:2), which are the C-terminal octapeptide sequences shared by all those consensus motifs of a ribbed mussel Geukensia demissa adhesive protein (RMAP), have been synthesized by the polycondensation of the active esters. The correlation between wettability and adhesion with the alternative substitution by hydrophobic Ala and hydrophilic Thr in the synthetic RMAPs in aqueous solution and as films on high and low surface free energy (sfe) surfaces has been investigated by surface chemical approaches. The side chain moieties of RMAPs arrange their local conformation to adapt to the inherent surface character, and they orientate on high and low sfe surfaces. On a high sfe glass the hydrophilic side chains of the RMAP molecules face toward the surface, and on a low sfe polyethylene (HDPE) the hydrophobic side chains face toward the surface. The bonding strengths of synthetic RMAPs on glass and HDPE with and without enzymatic oxidation have been examined. Increased starting concentration exhibited the strongest adhesive capability (7.5 kgf/cm2) on alumina due to the increased cohesion among RMAP molecules. As another factor to increase adhesive ability, the intermolecular cross-linking among RMAP molecules by tyrosinase increases their adhesive capability by about 20% on HDPE, glass, and alumina except iron.

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Section: Methodsmentioning

confidence: 99%

Synthesis and Wettability Characteristics of Model Adhesive Protein Sequences Inspired by a Marine Mussel

2000

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“…Since the specific rotation value of the hydrolysate of (1-6) agreed with that of authentic Ser(P), the possibility of the loss of chiral integrity during the polypeptide synthesis can be excluded. [26] Synthesis of Ser(P) Dipeptides [36] The compound 2-2 (4.2 g, 11.2 mmol) and 1 mol.-equiv. TEA in a 3-fold amount of chloroform was coupled with compounds 2-1 in a 3-fold amount of chloroform using DCCI (1.2 mol.-equiv.)…”

Section: Poly[ser(p)] (1-6)mentioning

confidence: 99%

Synthesis of Sequential Polypeptides Containing O‐Phospho‐L‐Serine

Yamamoto

Saitoh

Ohkawa

2003

Macromolecular Bioscience

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The chemistry of phosphoserine [Ser(P)] containing peptides and polypeptides was extensively investigated to explore a new biomineralization material science. The selective cleavage of the O,O′‐diphenyl phospho‐protecting groups of Ser(PO3Ph2) was examined using hydrogenolysis catalysts. Among the catalysts examined, only PtO2 in 50% trifluoroacetic acid (TFA)/AcOH successfully cleaved the protecting group of Ser(PO3Ph2) to give Ser(P). Based on these characteristic new findings, Ser(P)‐containing dipeptides such as Gly‐Ser(P), Ala‐Ser(P), Ser‐Ser(P), Asp‐Ser(P), Glu‐Ser(P), and Lys‐Ser(P), and tetrapeptide [Asp‐Ser(P)]2 were synthesized by a facile method. When we used the Ser(PO3Ph2) residues at the C terminals, the amino functional groups of amino acids and peptides can be coupled by the unsymmetric mixed anhydride using isobutyl chloroformate but cannot be by the symmetric anhydride method using dicyclohexylcarbodiimide. Neither unsymmetric mixed anhydride nor symmetric anhydride can be coupled with p‐nitrophenol at their C terminals. High‐molecular‐weight sequential polypeptides containing Ser(P) such as poly[Ser(P)‐Xaa] (Xaa: Gly, Ala, Ser, Lys, Asp, Glu) and poly[Gly‐Ser(P)‐Gly] were first synthesized by the polycondensation of the di‐ and tripeptide p‐nitrophenyl active esters, followed by the quantitative elimination of the diphenyl protecting groups by PtO2 in TFA/AcOH. The new strategy to synthesize Ser(P)‐containing peptides and model proteins may help the development of hybrid formulations of marine and biomimetic protein minerals.magnified image

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“…MATERIALS AND METHODS Syntheses of materials. The syntheses of the polymers (D-GIU'D-Ala )nL (Ala-'y-D-Glu-Lys-D-Ala-D-Ala)5 7 and (Ala-D-Glu-Lys-D-Ala-Gly)., as well as their tyrosylated and '25I-labeled analogs, have been previously reported (19,20). The haptens a-Boc-Lys-D-Ala-D-Ala, a-Boc-Lys-D-Ala-Gly, and Ala-D-Glu-Lys-D-Ala have also been synthesized and characterized (20,21).…”

mentioning

confidence: 99%

Antibody levels to bacterial peptidoglycan in human sera during the time course of endocarditis and bacteremic infections caused by Staphylococcus aureus

Zeiger¹,

Tuazon²,

Sheagren³

1981

Infect Immun

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Sera from patients with endocarditis and bacteremia due to Staphylococcus aureus were compared for peptidoglycan-binding capacity with those from normal blood donors. Those patients treated with beta-lactam antibiotics had higher antigen-binding levels than normal donors and patients treated exclusively with vancomycin (P less than 0.01). The factor responsible for this activity was purified by affinity chromatography from a normal donor and shown to be an immunoglobulin. Specificity studies indicated that the immunodominant determinant was a peptide sequence found in peptidoglycan precursors. Since soluble peptidoglycan molecules having the precursor peptide sequence are known to be secreted by some gram-positive bacteria like Micrococcus luteus when grown in the presence of beta-lactam antibiotics, these soluble molecules may constitute the "natural" immunogen. Such a hypothesis is consistent with the study of the peptidoglycan-binding capacities in the sera of these patients during the course of treatment. For most of the responding patients studied (four of four with bacteremia and seven of nine with endocarditis), a significant increase in peptidoglycan-binding capacity was observed in sera taken 1 to 5 weeks after the initiation of beta-lactam antibiotic therapy (compared with the initial serum studied). No such increase in the peptidoglycan-binding capacity over a similar time span was noted in the sera of people not receiving beta-lactam antibiotics (none of seven).

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Synthesis of two sequential polypeptides by dispersion in benzene and their circular dichroism spectra in aqueous solution: Poly(L‐Glu‐L‐Lys‐L‐Ala‐Gly) and Poly(L‐Ala‐D‐Glu‐L‐Lys‐D‐Ala‐Gly)

Cited by 16 publications

References 19 publications

Synthesis and Wettability Characteristics of Model Adhesive Protein Sequences Inspired by a Marine Mussel

Synthesis and Wettability Characteristics of Model Adhesive Protein Sequences Inspired by a Marine Mussel

Synthesis of Sequential Polypeptides Containing O‐Phospho‐L‐Serine

Antibody levels to bacterial peptidoglycan in human sera during the time course of endocarditis and bacteremic infections caused by Staphylococcus aureus

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