TY - JOUR
T1 - Synthesis of Peptoids Containing Multiple Nhtrp and Ntrp Residues
T2 - A Comparative Study of Resin, Cleavage Conditions and Submonomer Protection
AU - Lone, Abdullah
AU - Arnous, Anis
AU - Hansen, Paul Robert
AU - Mojsoska, Biljana
AU - Jenssen, Håvard
PY - 2020/4/29
Y1 - 2020/4/29
N2 - Peptoids hold status as peptide-mimetics with versatile biological applications due to their proteolytic stability and structural diversity. Among those that have been studied in different biological systems, are peptoids with dominant balanced hydrophobic and charge distribution along the backbone. Tryptophan is an important amino acid found in many biologically active peptides. Tryptophan-like side chains in peptoids allow H-bonding, which is absent from the parent backbone, due to the unique indole ring. Furthermore, the rigid hydrophobic core and flat aromatic system influence the positioning in the hydrocarbon core and allows accommodating tryptophan-like side chains into the interfacial regions of bacterial membranes and causing bacterial membrane damage. Incorporating multiple tryptophan-like side chains in peptoids can be tricky and there is a lack of suitable, synthetic routes established. In this paper, we investigate the synthesis of peptoids rich in Nhtrp and Ntrp residues using different resins, cleavage conditions, and unprotected as well as tert-butyloxycarbonyl-protected amines suitable for automated solid-phase submonomer peptoid synthesis protocols.
AB - Peptoids hold status as peptide-mimetics with versatile biological applications due to their proteolytic stability and structural diversity. Among those that have been studied in different biological systems, are peptoids with dominant balanced hydrophobic and charge distribution along the backbone. Tryptophan is an important amino acid found in many biologically active peptides. Tryptophan-like side chains in peptoids allow H-bonding, which is absent from the parent backbone, due to the unique indole ring. Furthermore, the rigid hydrophobic core and flat aromatic system influence the positioning in the hydrocarbon core and allows accommodating tryptophan-like side chains into the interfacial regions of bacterial membranes and causing bacterial membrane damage. Incorporating multiple tryptophan-like side chains in peptoids can be tricky and there is a lack of suitable, synthetic routes established. In this paper, we investigate the synthesis of peptoids rich in Nhtrp and Ntrp residues using different resins, cleavage conditions, and unprotected as well as tert-butyloxycarbonyl-protected amines suitable for automated solid-phase submonomer peptoid synthesis protocols.
KW - peptoids
KW - solid phase synthesis
KW - submonomer synthesis
KW - tryptamine
KW - tryptophan
U2 - 10.3389/fchem.2020.00370
DO - 10.3389/fchem.2020.00370
M3 - Journal article
SN - 2296-2646
VL - 8
JO - Frontiers in Chemistry
JF - Frontiers in Chemistry
IS - 8
M1 - 370
ER -