Halogenation dictates the architecture of amyloid peptide nanostructures
Pizzi, A.a, Pigliacelli, C.b, Gori, A.c, Nonappab, Ikkala, O.b, Demitri, N.d, Terraneo, G.a, Castelletto, V.e, Hamley, I.W.e, Baldelli Bombelli, F.a, Metrangolo, P.a,b,c
a Laboratory of Supramolecular and BioNano Materials (SupraBioNanoLab), Department of Chemistry, Materials, and Chemical Engineering Giulio Natta, Politecnico di Milano, Via Luigi Mancinelli 7, Milan, I-20131, Italy
b Department of Applied Physics, Aalto University, Espoo, FI-02150, Finland
c Istituto di Chimica Del Riconoscimento Molecolare-National Research Council of Italy (ICRM-CNR), Laboratory of Peptide and Protein Chemistry, Via Mario Bianco 9, Milan, 20131, Italy
d Elettra-Sincrotrone Trieste, S.S. 14 Km 163.5 in Area Science Park, Basovizza-Trieste, 34149, Italy
e Department of Chemistry, University of Reading, Whiteknights, Reading, RG6 6AD, United Kingdom
Amyloid peptides yield a plethora of interesting nanostructures though difficult to control. Here we report that depending on the number, position, and nature of the halogen atoms introduced into either one or both phenylalanine benzene rings of the amyloid β peptide-derived core-sequence KLVFF, four different architectures were obtained in a controlled manner. Our findings demonstrate that halogenation may develop as a general strategy to engineer amyloidal peptide self-assembly and obtain new amyloidal nanostructures.
