Structure optimization of lipopeptide assemblies for aldol reactions in an aqueous medium

Author(s):Show less -

Soares, Bruna M. ^[1] ; Sodre, Pedro T. ^[1] ; Aguilar, Andrea M. ^[2] ; Gerbelli, Barbara B. ^[1] ; Pelin, Juliane N. B. D. ^[1] ; Arguello, Karina B. ^[1] ; Silva, Emerson R. ^[3] ; de Farias, Marcelo A. ^[4] ; Portugal, Rodrigo V. ^[4] ; Schmuck, Carsten ^[5] ; Coutinho-Neto, Mauricio D. ^[1] ; Alves, Wendel A. ^[1]

Affiliation

^[1] Univ Fed ABC, Ctr Ciencias Nat & Humanas, BR-09210580 Santo Andre, SP - Brazil

^[2] Univ Fed Sao Paulo, Inst Ciencias Ambientais Quim & Farmaceut, BR-09972270 Diadema - Brazil

^[3] Univ Fed Sao Paulo, Dept Biofis, BR-04023062 Sao Paulo - Brazil

^[4] CNPEM, Brazilian Nanotechnol Natl Lab, BR-13083970 Campinas, SP - Brazil

^[5] Univ Duisburg Essen, Inst Organ Chem, D-45117 Essen - Germany

• Document type: Journal article
• Source: Physical Chemistry Chemical Physics; v. 23, n. 18, p. 10953-10963, MAY 14 2021.
• Web of Science Citations: 0

Abstract

Four amphiphilic peptides were synthesized, characterized, and evaluated regarding their efficiency in the catalysis of direct aldol reactions in water. The lipopeptides differ by having a double lipid chain and a guanidinium pyrrole group functionalizing one Lys side chain. All the samples are composed of the amino acids l-proline (P), l-arginine (R), or l-lysine (K) functionalized with the cationic guanidiniocarbonyl pyrrole unit (GCP), l-tryptophan (W), and l-glycine (G), covalently linked to one or two long aliphatic chains, leading to surfactant-like designs with controlled proline protonation state and different stereoselectivity. Critical aggregation concentrations (cac) were higher in the presence of the GCP group, suggesting that self-assembly depends on charge distribution along the peptide backbone. Cryogenic Transmission Electron Microscopy (Cryo-TEM) and Small Angle X-ray Scattering (SAXS) showed a rich polymorphism including spherical, cylindrical, and bilayer structures. Molecular dynamics simulations performed to assess the lipopeptide polymorphs revealed an excellent agreement with core-shell arrangements derived from SAXS data and provided an atomistic view of the changes incurred by modifying head groups and lipid chains. The resulting nanostructures behaved as excellent catalysts for aldol condensation reactions, in which superior conversions (>99%), high diastereoselectivities (ds = 94 : 6), and enantioselectivities (ee = 92%) were obtained. Our findings contribute to elucidate the effect of nanoscale organization of lipopeptide assemblies in the catalysis of aldol reactions in an aqueous environment. (AU)

• FAPESP's process: 17/02317-2 - Interfaces in materials: electronic, magnetic, structural and transport properties
• Grantee: Adalberto Fazzio
• Support Opportunities: Research Projects - Thematic Grants
• FAPESP's process: 18/05888-3 - Biosensors based on amphiphilic peptides for detection and diagnosis of diseases
• Grantee: Barbara Bianca Gerbelli
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• FAPESP's process: 15/20446-9 - Study of auto-organization in solution of hierarchical structures of peptide in presence of metallic nanoparticles
• Grantee: Juliane Nogueira Batista Dias Pelin
• Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
• FAPESP's process: 14/50867-3 - INCT 2014: National Institute of Science and Technology in Bioanalysis
• Grantee: Marco Aurelio Zezzi Arruda
• Support Opportunities: Research Projects - Thematic Grants