Doctoral Candidate
Chemistry

MS, Worcester Polytechnic Institute, 2002 (chemistry)
BS, Bogaziçi University, 2000 (chemistry)

Technological Institute K342
2145 Sheridan Road
Evanston, IL 60208-3113

(847) 491-4049 office/lab
(847) 491-3010 facsimile

Email Mustafa

Mustafa Guler

Recognition and Presentation of Biologically Active Groups on Peptide Ampihiphile Nanofibers

My research focuses on self-assembly properties of the biologically active peptide amphiphile systems (PAs) to study biological signals in the self-assembled structures. There are some limitations for the design and synthesis of new molecules. We research new synthetic ways for increasing the efficiency of the PA systems. Multiple presentations of epitopes, increasing the accessibility of various epitopes at the periphery of the PA nanofibers and modifying the self-assembly conditions are some of the new ways of making more efficient systems for biological studies. Recognition and accessibility of the bioactive groups on PA nanofibers are being tested with biotin-avidin binding. Figure 1 shows the molecular representation of the difference between a linear (a) and a branched system (b) in addition to avidin binding on a biotinylated PA nanofibers (c). Design and synthesis of new bioactive materials are under investigation.

Molecular Encapsulation in Peptide Amphiphile Nanofibers

The peptide amphiphiles with a hydrophobic segment and hydrophilic peptide sequence form nanofibers in water with the change of pH or in the presence of electrolytes. Hydrophobic part of the molecule is buried in the core of the nanofibers in water. This behavior is used to encapsulate hydrophobic molecules in the core of the nanofibers for possible drug delivery studies. Enzymatic reactions are also being studied to release the encapsulated molecules in the core of the PA nanofibers. In addition, single walled carbon nanotubes and some other hydrophobic molecules can also be encapsulated by these PA molecules.