Title :
Determination of binding effects of FN peptides with Platelet Derived Growth Factor (PDGF)
Author :
Fourman, M.S. ; Lin, F. ; Clark, R.A.
Author_Institution :
State Univ. of New York, Stony Brook
Abstract :
PDGF is a crucial growth factor in the human body, playing a part in cellular activity such as cell proliferation/migration, and angiogenesis. It is also linked to diseases such as atherosclerosis. Here we apply PDGF-BB to fibronectin domain binding. Four Peptides were tested originating from the first FN type III repeat (FNIII1), the heparinll-binding domain (FNIlI12-15) and the variably spliced IIICS domain. Circular dichroism was used to determine binding effects of PDGF to these peptides, evaluating the difference in signal between the addition of the independent peptides and the combination of the two. Results indicate distinct signal change in several of the target peptides when added to PDGF, indicating binding. Such results can also indicate as to positive beta-sheet secondary structure formation. This formation will be analyzed using Dichroweb software from the Centre for Protein and Membrane Structure and Dynamics (CPMSD) in Daresbury Laboratory. Results define binding trends of peptides to PDGF-BB, as well as clarify where binding on aforementioned domains best occurs.
Keywords :
biochemistry; cell motility; circular dichroism; molecular biophysics; proteins; Dichroweb software; FN peptides; angiogenesis; binding effects; cell migration; cell proliferation; cellular activity; circular dichroism; fibronectin; heparinll-binding domain; platelet derived growth factor; Absorption; Biological materials; Biomedical engineering; Biomedical materials; Buffer storage; Ice; Optical polarization; Peptides; Signal processing; Testing;
Conference_Titel :
Bioengineering Conference, 2007. NEBC '07. IEEE 33rd Annual Northeast
Conference_Location :
Long Island, NY
Print_ISBN :
978-1-4244-1033-0
Electronic_ISBN :
978-1-4244-1033-0
DOI :
10.1109/NEBC.2007.4413370