Andrew P. Laudano is a biochemistry researcher whose work with Russell F. Doolittle used synthetic peptides to investigate fibrin assembly. A historical university catalog records his UC San Diego doctorate in 1981 and lists him as an emeritus faculty member in 2013–2014.[ref]
Andrew P. Laudano entry in the University of New Hampshire 2013–2014 faculty catalog. Laudano,AndrewP entry: degree and historical faculty classification
In the 1978 experiment, Gly-Pro-Arg-Pro bound fibrinogen and fragment D but not the central fragment E. The shorter Gly-Pro-Arg bound less tightly and inhibited polymerization less effectively. These comparisons linked the structure of a small peptide to its ability to disrupt a larger molecular assembly.[ref]
Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization of fibrin monomers by Andrew P. Laudano and Russell F. Doolittle. Abstract: fragment-specific binding and tripeptide/tetrapeptide comparison
An illuminating control is a fragment that does not bind: it helps localize the interacting region rather than merely showing that “some protein” captures the peptide. Comparing related sequences adds another constraint. Together the tests connect binding affinity, molecular location and the observable formation of a fibrin network.
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