Molybdenum-Catalyzed Indane-Based Amino Acid/Peptide Synthesis

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

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A Strategy for Thioamide Incorporation During Fmoc Solid-Phase Peptide Synthesis with Robust Stereochemical Integrity

10.26434/chemrxiv.8206247.v1 ◽

2019 ◽

Cited By ~ 1

Author(s):

luis camacho III ◽

Bryan J. Lampkin ◽

Brett VanVeller

Keyword(s):

Amino Acid ◽

Functional Groups ◽

Peptide Synthesis ◽

Solid Phase ◽

Solid Phase Peptide Synthesis ◽

Side Chains ◽

Amino Acid Side Chains ◽

Peptide Elongation

We describe a method to protect the sensitive stereochemistry of the thioamide—in analogy to the protection of the functional groups of amino acid side chains—in order to preserve the thioamide moiety during peptide elongation.<br>

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Series of sequential polypeptides containing lysine or arginine: Preparation and characterization

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19880145 ◽

1988 ◽

Vol 53 (1) ◽

pp. 145-156 ◽

Cited By ~ 4

Author(s):

Jana Pírková ◽

Svetlana Churkina ◽

Vladimír Gut ◽

Ivo Frič ◽

Karel Bláha

Keyword(s):

Molecular Weight ◽

Amino Acid ◽

Peptide Synthesis ◽

Average Molecular Weight ◽

Basic Amino Acid ◽

Cd Spectra ◽

Active Esters ◽

Marked Tendency

The sequential polypeptides (Lys-Ala)n, (Lys-Ala-Ala)n, (Lys-Ala-Ala-Ala)n, (Lys-Leu-Ala)n, (Lys-Leu-Ala-Ala)n, (Lys-Leu-Ala-Ala-Ala)n, (Lys-Ala-Leu)n, (Lys-Ala-Leu-Ala)n, (Orn-Leu-Ala)n,(Arg-Ala-Ala)n, (Arg-Leu-Ala)n, (Arg-Leu-Ala-Ala)n, (Arg-Ala-Leu)n, and (Arg-Ala-Leu-Ala)n were synthesized by polymerization of active esters (1-succinimidyl or pentafluorophenyl) of the corresponding Nα-deblocked monomers. The monomers were prepared using the usual methods of peptide synthesis in solution. Upon dialysis, the average molecular weight of the polymer was 6 000-9 000 as determined by sedimentation in ultracentrifuge. Polypeptides, containing leucine in addition to the basic amino acid, showed a marked tendency to aggregation. CD spectra of the products were measured for characterization.

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Glucose phosphorylation. Interaction of a 50-amino acid peptide of yeast hexokinase with trinitrophenyl ATP.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)34124-9 ◽

1990 ◽

Vol 265 (9) ◽

pp. 5324-5328

Author(s):

K K Arora ◽

P Shenbagamurthi ◽

M Fanciulli ◽

P L Pedersen

Keyword(s):

Amino Acid ◽

Amino Acid Peptide ◽

Glucose Phosphorylation ◽

Yeast Hexokinase

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A C-peptide complex with albumin and Zn2+ increases measurable GLUT1 levels in membranes of human red blood cells

Scientific Reports ◽

10.1038/s41598-020-74527-6 ◽

2020 ◽

Vol 10 (1) ◽

Author(s):

M. Geiger ◽

T. Janes ◽

H. Keshavarz ◽

S. Summers ◽

C. Pinger ◽

...

Keyword(s):

Type 1 Diabetes ◽

Amino Acid ◽

Blood Cells ◽

Glucose Transporter ◽

Peptide Binding ◽

C Peptide ◽

Amino Acid Peptide ◽

Human Red Blood Cells

Abstract People with type 1 diabetes (T1D) require exogenous administration of insulin, which stimulates the translocation of the GLUT4 glucose transporter to cell membranes. However, most bloodstream cells contain GLUT1 and are not directly affected by insulin. Here, we report that C-peptide, the 31-amino acid peptide secreted in equal amounts with insulin in vivo, is part of a 3-component complex that affects red blood cell (RBC) membranes. Multiple techniques were used to demonstrate saturable and specific C-peptide binding to RBCs when delivered as part of a complex with albumin. Importantly, when the complex also included Zn2+, a significant increase in cell membrane GLUT1 was measured, thus providing a cellular effect similar to insulin, but on a transporter on which insulin has no effect.

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