Magnetically complexed tissue-mimicking peptides

2005 ◽  
Vol 97 (10) ◽  
pp. 10M521
Author(s):  
R. P. Guertin ◽  
R. Valluzzi ◽  
T. E. Haas ◽  
D. Pochan
Keyword(s):  
Mimicking Peptides

scholarly journals 1,2,3-Triazoles as Biomimetics in Peptide Science

Molecules ◽  
2021 ◽  
Vol 26 (10) ◽  
pp. 2937
Author(s):  
Naima Agouram ◽  
El Mestafa El Hadrami ◽  
Abdeslem Bentama
Keyword(s):  
Enzymatic Degradation ◽  
Triazole Ring ◽  
Biologically Active ◽  
Amide Bond ◽  
Biologically Relevant ◽  
Amide Bonds ◽  
Natural Peptides ◽  
Mimicking Peptides ◽  
Chemical Mediators

Natural peptides are an important class of chemical mediators, essential for most vital processes. What limits the potential of the use of peptides as drugs is their low bioavailability and enzymatic degradation in vivo. To overcome this limitation, the development of new molecules mimicking peptides is of great importance for the development of new biologically active molecules. Therefore, replacing the amide bond in a peptide with a heterocyclic bioisostere, such as the 1,2,3-triazole ring, can be considered an effective solution for the synthesis of biologically relevant peptidomimetics. These 1,2,3-triazoles may have an interesting biological activity, because they behave as rigid link units, which can mimic the electronic properties of amide bonds and show bioisosteric effects. Additionally, triazole can be used as a linker moiety to link peptides to other functional groups.

scholarly journals Back Cover: SUMO-Mimicking Peptides Inhibiting Protein SUMOylation (ChemBioChem 18/2014)

ChemBioChem ◽  
2014 ◽  
Vol 15 (18) ◽  
pp. 2792-2792
Author(s):  
Bo Zhao ◽  
Eric B. Villhauer ◽  
Karan Bhuripanyo ◽  
Hiroaki Kiyokawa ◽  
Hermann Schindelin ◽  
...  
Keyword(s):  
Back Cover ◽  
Inhibiting Protein ◽  
Mimicking Peptides ◽  
Protein Sumoylation

Mimicking Peptides… In Silico

2011 ◽  
Vol 31 (1) ◽  
pp. 12-20 ◽  
Author(s):  
Matteo Floris ◽  
Stefano Moro
Keyword(s):  
In Silico ◽  
Mimicking Peptides

scholarly journals A Histidine Switch in Hemagglutinin-Neuraminidase Triggers Paramyxovirus-Cell Membrane Fusion

2008 ◽  
Vol 83 (4) ◽  
pp. 1727-1741 ◽  
Author(s):  
Anuja Krishnan ◽  
Santosh K. Verma ◽  
Prashant Mani ◽  
Rahul Gupta ◽  
Suman Kundu ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Membrane Fusion ◽  
Fusion Proteins ◽  
Sendai Virus ◽  
Biological Activities ◽  
Viral Envelope ◽  
Attachment Protein ◽  
Histidine Residues ◽  
Human Parainfluenza Virus ◽  
Mimicking Peptides

ABSTRACT Most paramyxovirus fusion proteins require coexpression of and activation by a homotypic attachment protein, hemagglutinin-neuraminidase (HN), to promote membrane fusion. However, the molecular mechanism of the activation remains unknown. We previously showed that the incorporation of a monohistidylated lipid into F-virosome (Sendai viral envelope containing only fusion protein) enhanced its fusion to hepatocytes, suggesting that the histidine residue in the lipid accelerated membrane fusion. Therefore, we explored whether a histidine moiety in HN could similarly direct activation of the fusion protein. In membrane fusion assays, the histidine substitution mutants of HN (H247A of Sendai virus and H245A of human parainfluenza virus 3) had impaired membrane fusion promotion activity without significant changes in other biological activities. Synthetic 30-mer peptides corresponding to regions of the two HN proteins containing these histidine residues rescued the fusion promoting activity of the mutants, whereas peptides with histidine residues substituted by alanine did not. These histidine-containing peptides also activated F-virosome fusion with hepatocytes both in the presence and in the absence of mutant HN in the virosome. We provide evidence that the HN-mimicking peptides promote membrane fusion, revealing a specific histidine “switch” in HN that triggers fusion.

B-Cell Receptor Recognition of Multiple Epitopes Correlates with An Aggressive Clinical Course of Chronic Lymphocytic Leukemia.

Blood ◽  
2009 ◽  
Vol 114 (22) ◽  
pp. 56-56
Author(s):  
Mascha Binder ◽  
Antje Jackst ◽  
Barbara Léchenne ◽  
Fabian Mueller ◽  
Hendrik Veelken ◽  
...  
Keyword(s):  
Chronic Lymphocytic Leukemia ◽  
B Cell ◽  
Clinical Course ◽  
Lymphocytic Leukemia ◽  
Large Set ◽  
Epitope Recognition ◽  
Fab Fragments ◽  
Recognition Pattern ◽  
Aggressive Clinical Course ◽  
Mimicking Peptides

Abstract Abstract 56 INTRODUCTION: The malignant B-cells in chronic lymphocytic leukemia (CLL) express membrane immunoglobulins (B-cell receptors; BCR) which are specific for the leukemic clone of each individual patient. Emerging evidence suggests that the development and course of CLL may be driven by antigenic stimulation through the BCR. Here we set up a model system of epitope recognition in CLL to explore how diverse epitope recognition in CLL is and whether the epitope recognition pattern has clinical relevance. METHODS: BCRs from six randomly chosen CLL patients were cloned and recombinantly expressed as IgG1 Fab fragments. Combinatorial phage-displayed peptide libraries with five different insert designs were constructed and used for the selection of epitope-mimicking peptides on the Fab fragments. We tested the binding of phage displayed epitope mimics to the respective Fab fragment by ELISA as well as to the native BCR on the cells of CLL patients. Therefore, cell-bound phage displayed epitope mimics were separated from unbound phage by differential centrifugation and bound phage were quantified by bacterial infection. The binding of six ‘index‘ epitope mimics representative for each BCR was evaluated in a set of 100 unrelated CLL cell samples. Epitope recognition patterns of CLL BCRs were correlated with the clinical course of the disease by standard biostatistical analysis including Kaplan-Meier estimator, log-rank test, cox regression analysis and Chi-square test. RESULTS: We selected epitope-mimicking peptides from phage display libraries on six CLL BCRs from randomly chosen patients. The selected peptides bound to the recombinant BCRs as well as to the native BCRs on the respective CLL cells. To model epitope recognition in a larger cohort of CLL patients we chose six representative index epitope mimics and evaluated their binding in a large set of 100 unrelated CLL cases. Surprisingly, all CLL samples recognized one or several index epitopes. Some of the CLL samples showed marked polyreactivity whereas other samples were mono- or oligoreactive. We determined whether the degree of BCR polyreactivity correlates with the clinical course of the disease using time to first treatment (TTFT) as surrogate marker of disease progression. We found that CLL patients expressing BCRs reactive with each of the epitope mimics had a significantly worse clinical course than less reactive control patients (median TTFT 27 months versus 87 months). Moreover, CLL patients whose cells express BCRs reactive with five or more epitope mimics were also characterized by an aggressive clinical course as compared to patients reacting with less than five epitopes (median TTFT 24 months versus 97 months). These outcomes were unrelated to known prognostic markers such as BCR mutational status and high risk receptor configurations. CONCLUSIONS: We introduce a system for modelling and monitoring of BCR epitope reactivity in CLL. Our findings indicate that a polyreactive epitope recognition pattern may be a determinant of an aggressive clinical course in this disease. These findings further emphasize the functional and prognostic relevance of BCR epitope recognition patterns in CLL. Disclosures: No relevant conflicts of interest to declare.

Selection of Active ScFv to G-Protein-Coupled Receptor CCR5 Using Surface Antigen-Mimicking Peptides†

Biochemistry ◽  
2004 ◽  
Vol 43 (39) ◽  
pp. 12575-12584 ◽  
Author(s):  
Ying Zhang ◽  
Chadler Pool ◽  
Kristen Sadler ◽  
He-ping Yan ◽  
Jennifer Edl ◽  
...  
Keyword(s):  
G Protein ◽  
Surface Antigen ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled ◽  
Mimicking Peptides ◽  
Receptor Ccr5 ◽  
Selection Of
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