Although a lot of progress have been made in studying the molecules mechanism of peptide assembly, it remains a challenge to accurately regulate the assembly structure of peptides to achieve pre-designed structure and function. Chirality, an inherent property of peptides, has been recognized as a vital factor that can exert essential impacts on peptide assembly structures. In the development of peptide biomaterial, the chirality of peptide and amino acid residues is an important factor that has been taken into consideration by researchers. Numerous helical or twisted nanostructures and ordered ensembles have been successfully produced by molecular self-assembly from either single or multiple molecular components but it still remains a challenge to construct chiral nanostructures with desirable conformation (i.e., right-handed, P; left-handed, M) from specific chiral building blocks at will. Alternating D,L-oligopeptides are able to assume specific conformations including, among others, various kinds of single and double stranded β-helical structures. In previous study the conformational characteristics of Boc-(L-Val- D-Val)4-OMe in solution have been investigated by using NMR techniques. Different species that interconvert slowly compared with the proton spin time scale occur in chloroform solution and two of them are left-handed, doublestranded helical species of the type ↓↑β5.6 with 14 interstrand hydrogen bonds (Figure1). As illustrated in Figure 1 in the helix A the hydrogen bonds connect three pairs of D residues and four pairs of L residues, in the helix B the hydrogen bonds connect four pairs of D residues and three pairs of L residues. Note that the helix A can be converted into helix B (or vice versa) simply by transposing one strand by two residues with respect to the other. Here we report about synthesis and conformational behavior of a peptidic system that can be used for the removal of a wide variety of micropollutants of different size from natural and engineered water systems. References:[1] D.U. Römer, E. Fenude-Schoch, G.P. Lorenzi, Helvetica Chimica Acta (1993) 76, 451-458[2] G.P. Lorenzi, H. Jackle, L. Tomasic, V. Rizzo, C. Pedone, J. Am. Chem. Soc. (1985) 104, 1728-1733

Self-assembly as a molecular strategy of improve adsorbents of pollutants in water.

Fenude Emma
2023

Abstract

Although a lot of progress have been made in studying the molecules mechanism of peptide assembly, it remains a challenge to accurately regulate the assembly structure of peptides to achieve pre-designed structure and function. Chirality, an inherent property of peptides, has been recognized as a vital factor that can exert essential impacts on peptide assembly structures. In the development of peptide biomaterial, the chirality of peptide and amino acid residues is an important factor that has been taken into consideration by researchers. Numerous helical or twisted nanostructures and ordered ensembles have been successfully produced by molecular self-assembly from either single or multiple molecular components but it still remains a challenge to construct chiral nanostructures with desirable conformation (i.e., right-handed, P; left-handed, M) from specific chiral building blocks at will. Alternating D,L-oligopeptides are able to assume specific conformations including, among others, various kinds of single and double stranded β-helical structures. In previous study the conformational characteristics of Boc-(L-Val- D-Val)4-OMe in solution have been investigated by using NMR techniques. Different species that interconvert slowly compared with the proton spin time scale occur in chloroform solution and two of them are left-handed, doublestranded helical species of the type ↓↑β5.6 with 14 interstrand hydrogen bonds (Figure1). As illustrated in Figure 1 in the helix A the hydrogen bonds connect three pairs of D residues and four pairs of L residues, in the helix B the hydrogen bonds connect four pairs of D residues and three pairs of L residues. Note that the helix A can be converted into helix B (or vice versa) simply by transposing one strand by two residues with respect to the other. Here we report about synthesis and conformational behavior of a peptidic system that can be used for the removal of a wide variety of micropollutants of different size from natural and engineered water systems. References:[1] D.U. Römer, E. Fenude-Schoch, G.P. Lorenzi, Helvetica Chimica Acta (1993) 76, 451-458[2] G.P. Lorenzi, H. Jackle, L. Tomasic, V. Rizzo, C. Pedone, J. Am. Chem. Soc. (1985) 104, 1728-1733
2023
Istituto di Chimica Biomolecolare - ICB - Sede Pozzuoli
Peptide Assembly
Functional Peptide Materials
File in questo prodotto:
File Dimensione Formato  
prod_488144-doc_202988.pdf

solo utenti autorizzati

Descrizione: posterPepMat2023
Tipologia: Altro materiale allegato
Licenza: NON PUBBLICO - Accesso privato/ristretto
Dimensione 185.81 kB
Formato Adobe PDF
185.81 kB Adobe PDF   Visualizza/Apri   Richiedi una copia
Meeting Abstract P3_Fenude 2023.pdf

solo utenti autorizzati

Descrizione: Self-assembly as a molecular strategy of improve adsorbents of pollutants in water
Tipologia: Abstract
Licenza: NON PUBBLICO - Accesso privato/ristretto
Dimensione 888.53 kB
Formato Adobe PDF
888.53 kB Adobe PDF   Visualizza/Apri   Richiedi una copia

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/437228
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus ND
  • ???jsp.display-item.citation.isi??? ND
social impact