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SUMMARY:PhD Defense: Arvind Sathyavageeswaran\, " Designing Peptide-Based 
 Complex Coacervates for the Encapsulation of Globular Proteins”
DTSTART;VALUE=DATE-TIME:20260721T140000Z
DTEND;VALUE=DATE-TIME:20260721T153000Z
UID:217830456230
DESCRIPTION:Chair:  Sarah Perry\n\n"Designing Peptide-Based Complex Coace
 rvates for the Encapsulation of Globular Proteins”\n\nRecent work in bio
 logical condensates has highlighted the critical role of liquid-liquid pha
 se separation (LLPS) in cellular compartmentalization. Complex coacervates
  formed from oppositely charged polypeptides serve as excellent model syst
 ems to understand these membraneless phenomena. This work investigates the
  molecular design of peptide-based complex coacervates to understand how s
 equence\, charge density\, and hydrophobicity dictate phase behavior and m
 aterial properties. By utilizing rationally designed poly(lysine)- and pol
 y(glutamate)-based polypeptides\, we demonstrate that increasing charge bl
 ock size and hydrophobicity enhances coacervate stability against salt and
  increases viscosity. Furthermore\, we explore the encapsulation of model 
 proteins\, such as hen egg white lysozyme (HEWL)\, bovine serum albumin (B
 SA)\, and various supercharged green fluorescent protein (GFP) variants. T
 hese studies reveal that protein uptake is highly dependent on both the sp
 ecific charge distribution of the protein (e.g.\, patchy vs. isotropic) an
 d the sequence and hydrophobicity of the coacervating peptides. Additional
  studies on α-chymotrypsin (ChT) demonstrate that coacervate environments
  can be precisely tuned to modulate not only protein partitioning but also
  enzymatic activity. Ultimately\, these findings establish quantitative de
 sign rules for engineering synthetic membraneless organelles for biocataly
 sis\, protein stabilization\, and pharmaceutical applications.
LOCATION:LSL N410
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