Graphene for Amino Acid, Peptide, Protein, and Enzyme Detection

2014 ◽  
pp. 35-55
Author(s):  
Yuwei Hu ◽  
Fenghua Li ◽  
Dongxue Han ◽  
Li Niu
Keyword(s):  
Amino Acid ◽  
Amino Acid Peptide ◽  
Enzyme Detection

Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

1993 ◽  
Vol 51 ◽  
pp. 388-389
Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Vascular Tone ◽  
Cardiac Tissue ◽  
Ring Structure ◽  
Terminal Amino Acid ◽  
Amino Acid Peptide ◽  
Normal Human ◽  
Terminal Amino ◽  
The Brain

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.

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

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.

Ternary metal/nucleobase (oligonucleotide)/amino acid (peptide) complexes

1995 ◽  
Vol 59 (2-3) ◽  
pp. 147 ◽  
Author(s):  
H. Witkowski ◽  
I. Rombeck ◽  
T. Wienkötter ◽  
S. Höhmann ◽  
A. Erxleben ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Peptide ◽  
Ternary Metal ◽  
Peptide Complexes

scholarly journals In the Virion, the 11-Amino-Acid Peptide Cofactor pVIc Is Covalently Linked to the Adenovirus Proteinase

Virology ◽  
2002 ◽  
Vol 296 (2) ◽  
pp. 234-240 ◽  
Author(s):  
William J. McGrath ◽  
Katharine S. Aherne ◽  
Walter F. Mangel
Keyword(s):  
Amino Acid ◽  
Amino Acid Peptide ◽  
Covalently Linked

MS160 THE ANTI-INFLAMMATORY AND ANTIAPOPTOTIC ACTION OF HUMANIN – A NEWLY DISCOVERED 24-AMINO ACID PEPTIDE

2010 ◽  
Vol 11 (2) ◽  
pp. 141-142
Author(s):  
B. Zapala ◽  
A. Sliwa ◽  
J. Goralska ◽  
L. Kaczynski ◽  
I. Wybranska
Keyword(s):  
Amino Acid ◽  
Amino Acid Peptide ◽  
Anti Inflammatory

scholarly journals SYNTHESIS AND ANTIMICROBIAL EVALUATION OF QUINAZOLINONE PEPTIDE DERIVATIVES

2017 ◽  
Vol 10 (16) ◽  
pp. 7 ◽  
Author(s):  
Bhupinder Kapoor ◽  
Arshid Nabi ◽  
Reena Gupta ◽  
Mukta Gupta
Keyword(s):  
Antibacterial Activity ◽  
Amino Acid ◽  
Antimicrobial Agents ◽  
Methyl Esters ◽  
Standard Drug ◽  
Amino Acid Peptide ◽  
Chemical Structures ◽  
1H Nuclear Magnetic Resonance ◽  
Peptide Derivatives ◽  
Derivatives Of

  Objective: The increased microbial resistance against commercially available drugs initiated the development of novel and safe antimicrobial agents in last few decades. In this view, a series of amino acid/dipeptide derivatives of quinazolin-3(4H)-one was synthesized and was evaluated for their antimicrobial potential.Method: Synthesis of amino acid/peptide derivatives were carried out by coupling 5-(2-(2-chlorophenyl)-4-oxoquinazolin-3(4H)-yl)-2-hydroxy benzoic acid with amino acid/dipeptide methyl esters in the presence of dicyclohexylcarbodiimide and N-methylmorpholine. The chemical structures of synthesized compounds were characterized by 1H nuclear magnetic resonance and infrared spectroscopy and were screened for antibacterial activity by disc diffusion method.Results: All the synthesized derivatives exhibited moderate to significant antibacterial activity against both Gram-positive and Gram-negative bacteria. The potency of compound 5d was comparable to standard drug ciprofloxacin in all the strains of bacteria used. The compound 5a was found to be more active against Streptococcus pyogenes and Staphylococcus aureus while compound 5c against Pseudomonas aeruginosa and Escherichia coli. Conclusion: Peptide derivatives of quinazolinone are promising antimicrobial agent and can be used for the synthesis of other novel compounds.

scholarly journals Structural insights into the binding of the human receptor for advanced glycation end products (RAGE) by S100B, as revealed by an S100B–RAGE-derived peptide complex

2015 ◽  
Vol 71 (5) ◽  
pp. 1176-1183 ◽  
Author(s):  
Jaime L. Jensen ◽  
Venkata S. K. Indurthi ◽  
David B. Neau ◽  
Stefan W. Vetter ◽  
Christopher L. Colbert
Keyword(s):  
Amino Acid ◽  
Advanced Glycation End Products ◽  
Advanced Glycation ◽  
Amino Acid Peptide ◽  
Extracellular Milieu ◽  
Amino Terminal ◽  
Binding Interface ◽  
Glycation End Products ◽  
End Products ◽  
Type V

S100B is a damage-associated molecular pattern protein that, when released into the extracellular milieu, triggers initiation of the inflammatory response through the receptor for advanced glycation end products (RAGE). Recognition of S100B is accomplishedviathe amino-terminal variable immunoglobulin domain (V-domain) of RAGE. To gain insights into this interaction, a complex between S100B and a 15-amino-acid peptide derived from residues 54–68 of the V-domain was crystallized. The X-ray crystal structure was solved to 2.55 Å resolution. There are two dimers of S100B and one peptide in the asymmetric unit. The binding interface of this peptide is compared with that found in the complex between S100B and the 12-amino-acid CapZ-derived peptide TRTK-12. This comparison reveals that although the peptides adopt completely different backbone structures, the residues buried at the interface interact with S100B in similar regions to form stable complexes. The binding affinities of S100B for the intact wild-type V-domain and a W61A V-domain mutant were determined to be 2.7 ± 0.5 and 1.3 ± 0.7 µM, respectively, using fluorescence titration experiments. These observations lead to a model whereby conformational flexibility in the RAGE receptor allows the adoption of a binding conformation for interaction with the stable hydrophobic groove on the surface of S100B.

Sign in / Sign up

Export Citation Format

Share Document