Dr. Paul Weers

Dr. Paul Weers

Associate Professor (2003) 

Teaching: Biological Chemistry, Biochemistry Laboratory, Protein Biochemistry
E-mail: paul.weers@csulb.edu
Phone: 562.985.4948

Research Topics:

Apolipoproteins are the protein components of lipoproteins, and their role in lipid transport processes has been well documented. It is much less known that apolipoproteins also play an important role in innate immunity and our research program aims to understand this novel function. To study these critical players in lipid transport processes and innate immunity, we use an invertebrate apolipoprotein as a model system. This protein, apolipophorin III, has a known three-dimensional structure, which is critical to our structure-guided approach. Very few high resolution structures of human apolipoproteins are available, making our model system well suited for our research goals. Through a structure-guided site-directed mutagenesis approach we aim to obtain fundamental knowledge of how apolipoproteins function at the molecular level, gaining critical knowledge of their structure-function relationship. This allows us to understand the molecular basis of diseases associated with apolipoprotein function.


1. Wan, C.-P. L., Chiu, M.H., Wu, X, Lee, S., Prenner, E., and Weers, P.M.M. (2011) Apolipoprotein-induced conversion of SUVs into nanodisks. Biochim. Biophys. Acta (Biomembranes) 1808, 606-613.

2. Weers, P.M.M., Patel, A.B., Wan, L.C.-P., Guigard, E., Kay, C.M., Hafiane, A., McPherson, R., Marcel, Y.L., Kiss, R.S. (2011) Novel N-terminal mutation of human apolipoprotein A-I reduces self-association and impairs LCAT activation. J. Lipid Res. 52, 35-44.

3. Narayanaswami, V., Kiss, R.S., Weers, P.M.M. (2010) Review, The helix bundle: a reversible lipid binding motif. Comparative Biochemistry Physiology A. Mol. Integr. Physiol. 155, 123-133.

4. Chiu, M.C., Wan, C.-P. L., Weers, P.M.M., Prenner, E.J. (2009) Apolipophorin III interaction with model membranes composed of phosphatidylcholine and spingomyelin using differential scanning calorimetry. Biochim. Biophys Acta (Biomembranes) 1788, 2160-2168.

5. Vasquez, L.J., Abdullahi, G.E., Wan, C.-P. L., Weers, P.M.M. (2009) Apolipophorin III lysine modification: effect on structure and lipid binding. Biochim. Biophys Acta (Biomembranes), 1788, 1901-1906.

6. Hauser, P.S., Raussens, V., Yamamoto, T., Abdullahi, G.E., Weers, P.M.M., Sykes, B.D., and Ryan R.O. (2009) Semisynthesis and segmental isotope labeling of apoE3 N-terminal domain using expressed protein ligation. J. Lipid Res. 50, 1548-1555.

7. Wong, K., Beckstead, J.A., Lee, D., Weers, P.M.M., Guigard, E., Kay, C.M., and Ryan, R.O. (2008) The N-terminus of apolipoprotein A-V adopts a helix bundle molecular architecture, Biochemistry 47, 8768-74.

8. Nguyen, T.-S., Weers, P.M.M., Raussens, V., Wang, Z., Ren, G., Sulchek, T., Hoeprich, P.D., and Ryan, R.O. (2008) Amphotericin B induced interdigitation of apolipoprotein stabilized nanodisk bilayers. Biochim. Biophys. Acta 1778, 3033-312.

9. Beckstead, J.A., Wong, K., Gupta, V., Wan, C.-P. L., Cook, V.R., Weinberg, R.B., Weers, P.M.M. and Ryan, R.O. (2007) The C terminus of apolipoprotein A-V modulates lipid-binding activity. J. Biol. Chem. 282, 15484-15489.

10. Leon, L.J., Idangodage, H., Wan, L. C.-P, and Weers, P.M.M. (2006) Apolipophorin III: lipopolysaccharide binding requires helix bundle opening. Biochem. Biophys. Res. Commun. 348, 1328-1322.

11. Leon, L.J., Pratt, C.C., Vasquez, L.J., and Weers, P.M.M. (2006) Tyrosine fluorescence analysis of apolipophorin III . lipopolysaccharide interaction. Arch. Biochem. Biophys. 452, 38-45.

12. Weers, P.M.M., and Ryan, R.O. (2006) Apolipophorin III: role model apolipoprotein. Insect Biochem. Mol. Biol. 36, 231-240.

13. Weers, P.M.M., Cabrera, J., Abdullahi, W.E., and Hsu, T.-C. (2005) Role of buried polar residues in helix bundle stability and lipid binding of apolipophorin III: destabilization by threonine 31. Biochemistry 44, 8810-8816.

14. Pratt, C.C., and Weers, P.M.M. (2004) Lipopolysaccharide binding of an exchangeable apolipoprotein, apolipophorin III from Galleria mellonella. Biol. Chem. 385, 1113-1119.