Lawrence Livermore National Security, LLC

Julio A Camarero

James J De Yoreo

Youngeun Kwon

Paul D Hoeprich

Alexander R Mitchell

James J DeYoreo

Synthetic apolipoproteins based on native/naturally occurring homolog proteins can be prepared using solid-phase peptide synthesis approaches combined with native chemical ligation methods to create analogs of full length apolipoproteins. The chemical synthesis is expected to allow introduction of non-natural amino acids, e.g., &#x3b1;,&#x3b1;'-dialkyl amino acids, with a periodicity that encourages both helix formation and amphipathicity. Such apolipoprotein analogs are expected to encourage, in some embodiments, facile and more complete NLP formation, enabling consideration of full spectrum of nanoparticle-based biotechnology applications ranging from therapeutic sequestration and delivery to energy/biofuel production to biopolymer production.

Synthetic apolipoproteins, and related compositions methods and systems for nanolipoprotein particles formation

Described herein is a method for the attachment of proteins to any solid support with control over the orientation of the attachment. The method is extremely efficient, not requiring the previous purification of the protein to be attached, and can be activated by UV-light. Spatially addressable arrays of multiple protein components can be generated by using standard photolithographic techniques.

Photoswitchable method for the ordered attachment of proteins to surfaces

Disclosed herein is a new method for the solid phase peptide synthesis (SPPS) of C-terminal peptide &#x3b1; thioesters using Fmoc/t-Bu chemistry. This method is based on the use of an aryl hydrazine linker, which is totally stable to conditions required for Fmoc-SPPS. When the peptide synthesis has been completed, activation of the linker is achieved by mild oxidation. The oxidation step converts the acyl-hydrazine group into a highly reactive acyl-diazene intermediate which reacts with an &#x3b1;-amino acid alkylthioester (H-AA-SR) to yield the corresponding peptide &#x3b1;-thioester in good yield. A variety of peptide thioesters, cyclic peptides and a fully functional Src homology 3 (SH3) protein domain have been successfully prepared.

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Livermore, CA, United States of America

Julio A Camarero