TY - GEN
T1 - Determination of binding effects of FN peptides with platelet derived growth factor (PDGF)
AU - Fourman, M. S.
AU - Lin, F.
AU - Clark, R. A.
PY - 2007
Y1 - 2007
N2 - 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 heparinII-binding domain (FNIII12-15) 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 will define binding trends of peptides to PDGF-BB, as well as clarify where binding on aforementioned domains best occurs.
AB - 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 heparinII-binding domain (FNIII12-15) 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 will define binding trends of peptides to PDGF-BB, as well as clarify where binding on aforementioned domains best occurs.
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U2 - 10.1109/NEBC.2007.4413370
DO - 10.1109/NEBC.2007.4413370
M3 - Conference contribution
AN - SCOPUS:48749103012
SN - 1424410339
SN - 9781424410330
T3 - Proceedings of the IEEE Annual Northeast Bioengineering Conference, NEBEC
SP - 247
EP - 248
BT - 33rd Annual Northeast Bioengineering Conference - Engineering Innovations in Life Sciences and Healthcare, NEBC
PB - Institute of Electrical and Electronics Engineers Inc.
T2 - 33rd Annual Northeast Bioengineering Conference, NEBC
Y2 - 10 March 2007 through 11 March 2007
ER -
