Structural and Positional Studies of the

Antimicrobial Peptide Brevinin-1BYa in

Membrane-Mimetic Environments -
Supplementary Information

Patrick Brendan Timmons1 , Donal O’Flynn2 ,

J. Michael Conlon3 , Chandralal M. Hewage1†

1
UCD School of Biomolecular and Biomedical Science, UCD Centre for
Synthesis and Chemical Biology, UCD Conway Institute, University College
Dublin, Dublin 4, Ireland
2
ProVerum Medical Limited, Trinity Translational Medicine Institute,
Trinity Centre for Health Sciences, St James’s Hospital, Dublin 8, Ireland
3
Diabetes Research Group, School of Biomedical Sciences, Ulster
University, Cromore Road, Coleraine, Northern Ireland
†
chandralal.hewage@ucd.ie

1
Table 1: 1 H chemical shifts (ppm) identified for every residue of brevinin-
1BYa in 33% TFE-d3 /H2 O

Amino acid NH Hα Hβ Other protons

Phe1 4.31 3.26
Leu2 7.90 4.73 1.63 γ 1.56, δ 0.97
Pro3 4.45 2.36, 2.08 γ 2.10, δ 3.80, 3.55
Ile4 7.58 4.05 1.92 γ 1 1.57, 1.30, γ 2 0.98
Leu5 7.50 4.18 1.72 δ 1.00, 0.92,
Ala6 7.73 4.12 1.52
Ser7 7.84 4.27 4.09, 3.98
Leu8 8.03 4.26 2.05, 1.63 γ 1.92, δ 0.95,
Ala9 8.50 4.07 1.45
Ala10 7.88 4.15 1.54
Lys11 7.62 4.15 1.72, 1.53 γ 1.17, 0.97, δ 1.54, CH 2 2.89, 2.84, N H 3 7.57
Phe12 8.40 4.72 3.24, 2.98 δ 7.34
Gly13 8.32 4.36, 4.00
Pro14 4.41 2.43, 2.06 γ 2.13, δ 3.87, 3.74
Lys15 7.83 4.17 2.02, 1.98 γ 1.63, δ 1.80, CH 2 3.05
Leu16 8.04 4.07 1.78, 1.66 δ 0.88
Phe17 7.91 4.14 3.21 δ 7.18,  7.28
Cys18 8.06 4.33 3.28, 3.11
Leu19 7.97 4.12 1.86, 1.66 γ 1.67, δ 0.80, 0.75
Val20 8.18 3.80 2.04 γ 1.02, 0.91
Thr21 7.79 4.12 4.03 γ 0.91
Lys22 7.94 4.22 2.21, 2.16 γ 1.43, δ 1.78, CH 2 3.09, N H 3 7.58
Lys23 7.79 4.46 2.08, 1.72 γ 1.45, δ 1.70, CH 2 3.08, N H 3 7.58
Cys24 7.80 4.50 3.47

2
Table 2: 1 H chemical shifts (ppm) identified for every residue of brevinin-
1BYa in SDS micelles

Amino acid NH Hα Hβ Other protons

Phe1 4.47 3.18
Leu2 7.85 4.65 1.64
Pro3 4.31 2.33, 2.06 γ 2.17, δ 3.97, 3.77
Ile4 8.20 4.08 2.09 γ 1 1.59, 1.28, γ 2 0.91
Leu5 7.55 4.08 1.87, 1.77 γ 1.58
Ala6 8.14 4.06 1.53
Ser7 7.97 4.26 4.04, 4.00
Leu8 8.18 4.20 2.06, 1.58 δ 1.01
Ala9 8.61 3.93 1.51
Ala10 7.85 4.10 1.50
Lys11 7.53 4.06 1.65, 1.40 γ 1.39
Phe12 8.38 4.75 3.24, 2.86  7.28
Gly13 8.50 4.27, 3.83
Pro14 4.27 2.46, 1.90 γ 2.17, δ 3.71, 3.50
Lys15 7.17 4.15 2.08, 2.00 γ 1.58, δ 1.81
Leu16 8.22 4.12 1.78 δ 0.93
Phe17 8.74 4.05 3.32, 3.12 δ 7.11,  7.29
Cys18 8.18 4.29 3.24, 3.09
Leu19 8.13 4.16 1.92, 1.75 γ 1.76, δ 0.93
Val20 8.01 3.85 2.04 γ 1.04, 0.92
Thr21 7.73 4.16 3.98 γ 0.85
Lys22 7.89 4.23 2.08 γ 1.37
Lys23 7.61 4.36 2.00, 1.65 γ 1.38
Cys24 7.83 4.40 3.46, 3.37

3
Table 3: 1 H chemical shifts (ppm) identified for every residue of brevinin-
1BYa in DPC micelles

Amino acid NH Hα Hβ Other protons

Phe1 4.30 3.31, 3.18 δ 7.31
Leu2 4.37
Pro3 4.35 2.36, 2.00 γ 2.12, δ 3.81, 3.75
Ile4 8.26 4.06 1.99 γ 1 1.58, 1.28
Leu5 7.79 4.06 1.75 γ 1.61, δ 0.95
Ala6 8.22 4.01 1.53
Ser7 7.97 4.25 4.01, 3.96
Leu8 8.14 4.20 2.03, 1.50 γ 1.56, δ 0.98
Ala9 8.56 3.92 1.49
Ala10 7.92 4.07 1.50
Lys11 7.55 4.06 1.65, 1.39 δ 1.05, 0.64, CH 2 2.75
Phe12 8.33 3.22, 2.86 δ 7.29,  7.32
Gly13 8.41 4.25, 3.82
Pro14 4.24 2.44, 1.89 γ 2.20, δ 3.70, 3.54
Lys15 7.31 4.16 2.06, 1.95 δ 1.78, CH 2 2.98
Leu16 8.21 4.10 1.78 δ 0.91
Phe17 8.65 4.04 3.35, 3.09 δ 7.12,  7.28
Cys18 8.22 4.30 3.24, 3.12
Leu19 8.10 4.15 1.93, 1.79 γ 1.67, δ 0.91
Val20 7.91 3.86 2.05 γ 1.02
Thr21 7.68 4.12 3.99 γ 0.81
Lys22 7.95 4.16 2.06 δ 1.37
Lys23 7.67 4.40 1.98, 1.64 γ 1.38, δ 1.70, CH 2 3.00
Cys24 7.80 4.42 3.42