A ?-turn mimic and a thiomethylene dipeptide surrogate employed in the study of cyclic peptide RGD and RCD cell-adhesion inhibitors

1996 ◽  
Vol 3 (1) ◽  
pp. 37-44
Author(s):  
Gilbert M. Rishton ◽  
Nancy K. Harn ◽  
Stephan J. Cripps ◽  
Shiu-Lan Chiang ◽  
Christy Mikos ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cyclic Peptide ◽  
Turn Mimic ◽  
Peptide Rgd

Structural and ICAM-1-Docking Properties of a Cyclic Peptide from the I-domain of LFA-1: An inhibitor of ICAM-1/LFA-1-mediated T-cell adhesion

2002 ◽  
Vol 19 (5) ◽  
pp. 789-799 ◽  
Author(s):  
Christine R. Xu ◽  
Helena Yusuf-Makagiansar ◽  
Yongbo Hu ◽  
Seetharama D.S. Jois ◽  
Teruna J. Siahaan
Keyword(s):  
Cell Adhesion ◽  
T Cell ◽  
Cyclic Peptide ◽  
T Cell Adhesion

Impact of bifunctional chelators on biological properties of 111In-labeled cyclic peptide RGD dimers

Amino Acids ◽  
2010 ◽  
Vol 41 (5) ◽  
pp. 1059-1070 ◽  
Author(s):  
Jiyun Shi ◽  
Young-Seung Kim ◽  
Sudipta Chakraborty ◽  
Yang Zhou ◽  
Fan Wang ◽  
...  
Keyword(s):  
Cyclic Peptide ◽  
Biological Properties ◽  
Bifunctional Chelators ◽  
Peptide Rgd

A Ca2+binding cyclic peptide derived from the ?-subunit of LFA-1: inhibitor of ICAM-1 /LFA-1-mediated T-cell adhesion

1999 ◽  
Vol 53 (1) ◽  
pp. 18-29 ◽  
Author(s):  
S. D. S. Jois ◽  
T. J. Siahaan ◽  
S. A. Tibbetts ◽  
M. A. Chan ◽  
S. H. Benedict
Keyword(s):  
Cell Adhesion ◽  
T Cell ◽  
Cyclic Peptide ◽  
T Cell Adhesion

scholarly journals Adhesion, proliferation and viability of human umbilical vein endothelial cells cultured on the surface of biodegradable non-woven matrices modified with RGD peptides

2019 ◽  
Vol 21 (1) ◽  
pp. 142-152 ◽  
Author(s):  
L. V. Antonova ◽  
V. N. Silnikov ◽  
M. Yu. Khanova ◽  
L. S. Koroleva ◽  
I. Yu. Serpokrilova ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cell Adhesion ◽  
Laser Scanning ◽  
Cyclic Peptide ◽  
Umbilical Vein ◽  
Small Diameter ◽  
Laser Scanning Microscopy ◽  
Rgd Peptides ◽  
Human Umbilical Vein ◽  
Cells Cultured

Tissue engineering is a promising area for the production of small-diameter vascular grafts. In recent years, a number of strategies have been developed to make the polymer surfaces of vascular prostheses capable to selectively adhesion of endothelial cells. The arginine–glycine–aspartic acid (RGD) sequence (a cell adhesion site that is present on many extracellular matrix proteins) is the promising target for modification. The efficiency of attachment of endothelial cells can be influenced both by the structure of RGD peptide and the extent of linker group.Aim: to determine the optimal method for modification of non-woven matrices of polyhydroxybutyrate/ valerate and polycaprolactone (PHBV/PCL) by RGD-peptides leading to the increasing of adhesion, viability and proliferation of endothelial cells.Materials and methods. Electrospinning was used to produce 4 mm diameter tubular polymer matrices from PHBV/PCL. Modification of surface of polymer scaffolds was performed using 4,7,10-trioxa-1,13-tridekandiamin, hexamethylenediamine, glutaraldehyde, ninhydrin, ascorbic acid, a cyclic peptide c [RGDFK], RGDK, AhRGD. The quality of modification was assessed by ninhydrin test and determination of arginine-containing peptide. The structure of the surface of matrices before and after modification was studied by scanning electron microscopy. Adhesion, viability and proliferation of Human umbilical vein (HUVEC) endothelial cells cultured for 7 days on the surface of matrices in the presence of RGD and without one were examined using fluorescence and laser scanning microscopy after the cells were pre-stained with fluorescent nuclear dyes (ethidium bromide and Hoechst 33342), and also by special kits for proliferation assessment (Click-iTTM Plus EdU Alexa FluorTM 488 Imaging Kit).Results. RGD peptides bound to the matrix surface via a long linker (4,7,10-trioxa-1,13-tridecanediamine) were characterized by the increased bioavailability and activity. High level of cell adhesion, viability and proliferation were noted on the surface of RGDK and c[RGDFK] modified matrices, whereas their paired analogues with a short linker (hexamethylenediamine) showed low results of cellular viability even against satisfactory cell adhesion.Discussion. Non-woven matrices based on PHBV/PCL and modified using 4,7,10-trioxa-1,13-tridecanediamine showed better results in case of adhesion of HUVEC and subsequent preservation of cell viability and proliferation. RGD-containing peptides of RGDK and c [RGDFK] were more tropic to endothelial cell receptors.

Adhesion of Hairy Cells Leukemia (HCL) Cells to Stromal Cells Can Be Inhibited by Blocking VLA-4 Integrins and CXCR4 Chemokine Receptors

Blood ◽  
2011 ◽  
Vol 118 (21) ◽  
pp. 1760-1760 ◽  
Author(s):  
Mariela Sivina ◽  
Robert J. Kreitman ◽  
Amnon Peled ◽  
Farhad Ravandi ◽  
Jan A. Burger
Keyword(s):  
Bone Marrow ◽  
Cell Adhesion ◽  
Lymph Nodes ◽  
Adhesion Molecules ◽  
Cell Lines ◽  
Chemokine Receptors ◽  
Cyclic Peptide ◽  
Conflicts Of Interest ◽  
Binding Motif ◽  
Hairy Cells

Abstract Abstract 1760 Hairy cell leukemia (HCL) has a unique pattern of tissue infiltration by the HCL cells, causing splenomegaly and marrow infiltration, but rarely affecting the lymph nodes, or causing a significant leukemic involvement. Chemokine receptors and adhesion molecules play key roles in normal B cell trafficking and homing to different tissue microenvironments, and expression of these molecules on hairy cells is thought to function in a similar fashion, regulating the trafficking of hairy cells between the blood, spleen, and bone marrow. In this study, we profiled the expression and function of chemokine receptors (CXCR4, CXCR5, CXCR3, CCR7) and adhesion molecules (CD49d/VLA-4, CD54/ICAM-1, CD44, and CD62L) in primary HCL cells and HCL cell lines (Bonna-12, HC-1 and ESKOL). Primary HCL cells from 9 different patients displayed high levels of CD49d/VLA-4, CD54/ICAM-1, CXCR4, CD44, CD103 and CD11c; only in few cases we found a small sub-population of cells expressing CXCR5. Cell adhesion molecules like CD62L and the chemokine receptors CCR7 that are critical for entry and positioning in lymph nodes were not expressed in any of the analyzed samples. Similar immunophenotypic profiles were found in the HCL cell lines, with the exception of CD103 and CD11c, which were not expressed on the HCL cell lines. Bone marrow stroma cells (BMSC) constitutively secrete CXCL12 and provide ligands for VLA-4 integrins, and thereby may attract and retain HCL cells in the marrow. Also, these two molecules can be clinically targeted using small molecule antagonists or monoclonal antibodies (mAbs). Therefore, we analyzed HCL cell migration and adhesion towards BMSC (R-15C and Tst-4) after 4 hours of co-culture. As documented via phase contrast microscopy and quantified by flow cytometry, HCL cell lines and primary HCL cells showed abundant adhesion and migration beneath BMSC. Next, we examined whether blocking of CXCR4 using the CXCR4 antagonists AMD3100 and BKT-140 or blocking of VLA-4 integrins using CS-1 peptides affects this adhesion of HCL cells to BMSC. Pre-incubation with AMD3100 significantly reduced BMSC adhesion of hairy cells to levels that were 70.6 ±7.8% (p<0.05) of controls using Tst-4 BMSC. Similar results were found when hairy cells were pre-incubated with the CXCR4 antagonist BKT-140 (65.4 ± 10.6%, p<0.05, n=7). Interestingly, when hairy cells were pretreated with a cyclic peptide inhibitor with a minimal VLA-4 binding motif “LDV” (CS-1 peptide), a significant reduction of HCL cell adhesion was also found, reducing HCL cell adhesion to 53.0 ± 9.7% of controls (p< 0.01) with Tst-4 BMSC; similar results were found using R-15C BMSC, as shown in the Figure. In a preliminary study, with 4 cases analyzed, we also found that co-culture of primary HCL cells with BMSC improved HCL cell survival, as assessed by staining with DiOC6 and PI. BMSC co-culture increased the proportion of viable HCL cells to 134 ± 13% (n=4) of the control (HCL in culture without BMSC) on day 2 and to 252 ± 72% (n=2) on day 4. Collectively, our studies provide insight into the molecular interactions between HCL cells and BMSC and provide an explanation for the distinct pattern of tissue infiltration in HCL. Also, they provide a rationale for further preclinical development of CXCR4 and VLA-4 antagonists in HCL. Disclosures: No relevant conflicts of interest to declare.

scholarly journals Synthesis of an σ-dehydro β-amino acid derived cyclic peptide as a constrained  β-turn mimic

ARKIVOC ◽  
2001 ◽  
Vol 2001 (8) ◽  
pp. 20-26
Author(s):  
S. Rajesh ◽  
Jyoti Srivastava ◽  
Biswadip Bannerji ◽  
Javed Iqbal
Keyword(s):  
Amino Acid ◽  
Cyclic Peptide ◽  
Turn Mimic
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