Table 1 Peptides sequence, molecular characterization, and physiochemical properties84.

From: Molecular hybridization strategy for tuning bioactive peptide function

Label

Peptide

Sequencea

Molecular weight (Da)

H

µH

z

P/N

Theoretical

Observed

V

VmCT1

Phe-Leu-Gly-Ala-Leu-Trp-Asn-Val-Ala-Lys-Ser-Val-Phe

1450.7

1451

0.82

0.58

+2

0.50

A

Anoplin

Gly-Leu-Leu-Lys-Arg-Ile-Lys-Thr-Leu-Leu

1152.5

1153

0.59

0.71

+4

1.00

AV

Anoplin-VmCT1

Gly-Leu-Gly-Ala-Leu-Leu-Asn-Val-Ile-Lys-Ser-Gly-Leu

1253.5

1254

0.65

0.55

+2

0.86

P

Protonectin

Ile-Leu-Gly-Thr-Ile-Leu-Gly-Leu-Leu-Lys-Gly-Leu

1209.6

1210

0.95

0.68

+2

0.71

PV

Protonectin-VmCT1

Ile-Leu-Gly-Ala-Ile-Leu-Asn-Val-Leu-Lys-Ser-Leu-Gly

1309.6

1310

0.77

0.66

+2

0.62

VP

VmCT1-Protonectin

Phe-Leu-Gly-Thr-Leu-Trp-Gly-Gly-Ala-Lys-Gly-Val-Phe

1351.6

1351

0.77

0.52

+2

0.86

D

Decoralin

Ser-Leu-Leu-Ser-Leu-Ile-Arg-Lys-Leu-Ile-Thr

1254.8

1256

0.78

0.65

+3

0.83

DV

Decoralin-VmCT1

Ser-Leu-Gly-Ala-Leu-Ile-Asn-Val-Leu-Lys-Ser-Gly-Gly

1227.4

1229

0.52

0.46

+2

1.16

VD

VmCT1-Decoralin

Phe-Leu-Gly-Ser-Leu-Trp-Arg-Lys-Ala-Gly-Thr-Val-Phe

1480.7

1481

0.69

0.58

+4

0.86

T

Temporin A

Phe-Leu-Pro-Leu-Ile-Gly-Arg-Val-Leu-Ser-Gly-Ile-Leu

1396.8

1397

1.00

0.61

+2

0.44

TV

Temporin A-VmCT1

Phe-Leu-Gly-Ala-Ile-Gly-Asn-Val-Leu-Lys-Ser-Ile-Leu

1343.7

1344

0.80

0.71

+2

0.62

VT

VmCT1-Temporin A

Phe-Leu-Pro-Leu-Leu-Trp-Arg-Val-Ala-Ser-Gly-Val-Phe

1503.8

1504

1.00

0.47

+2

0.30

  1. H hydrophobicity, μH hydrophobic moment, z net charge, P/N ratio of polar/non-polar residues in the sequence. Underlines highlight Gly residues that were inserted so all peptides would have matching hydrophobic and hydrophilic faces in the helical wheel projections.
  2. H, μH, z, and P/N according to helical wheel projection server Heliquest84.
  3. Mass obtained under the following conditions: Phenomenex Gemini C18column (2.0 mm × 150 mm, 3.0 µm particles, 110 Å pores). Solvent A was 0.1% TFA in water, and solvent B was 90% ACN in solvent A. Elution with a 5–95% B gradient was performed over 20 min, 0.2 mL min−1 flow, and peptides were detected at 220 nm. Mass measurements were performed in a positive mode with the following conditions: mass range between 100 and 2500 m/z, ion energy of 5.0 V, nitrogen gas flow of 12.0 L min−1, solvent heater of 250 °C, multiplier of 1.0, capillary of 3.0 kV and cone voltage of 35 V.
  4. Amino acid residues highlighted in bold are originally from VmCT1’s sequence.
  5. aAll sequences present amidated C-terminus.
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