Side-chain alanine-based block copolymer as natural product delivery system

Amyloid β-Peptide Segment Conjugated Side-Chain Proline-Based Polymers as Potent Inhibitors in Lysozyme Amyloidosis

“…Their reduced susceptibility to proteolysis, enhanced aqueous solubility, rational design, and peptide mimetic behavior 14 small molecules. 15,16 During peptide shortlisting, it is noted that amyloids are rich in β-sheets that are held through Hbonding and are strongly stabilized by hydrophobic interactions, 17,18 regardless of their origin and sequence of unfolded peptides. The importance of hydrophobic interactions is realized from both amyloids promoting a selfrecognition unit (12−17) hydrophobic region of islet amyloid polypeptide (IAPP) 19 in T2D and central hydrophobic core (16−20) KLVFF of amyloid beta (Aβ) peptide.…”

“…In this milieu, taking advantage of both small molecules, such as amino acids and peptides, and using the advanced polymerization techniques to design biocompatible side-chain amino acid-based peptide–polymer bioconjugate inhibitors hold significant promise. Their reduced susceptibility to proteolysis, enhanced aqueous solubility, rational design, and peptide mimetic behavior make them superior for targeting with increased bioavailability and multivalency compared to small molecules. , During peptide shortlisting, it is noted that amyloids are rich in β-sheets that are held through H-bonding and are strongly stabilized by hydrophobic interactions, , regardless of their origin and sequence of unfolded peptides. The importance of hydrophobic interactions is realized from both amyloids promoting a self-recognition unit (12–17) hydrophobic region of islet amyloid polypeptide (IAPP) in T2D and central hydrophobic core (16–20) KLVFF of amyloid beta (Aβ) peptide.…”