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. 2020 Jan 20;10:690. doi: 10.1038/s41598-019-57229-6

Table 1.

Properties of potato peptides predicted by bioinformatics to have emulsifying activity.

Peptide Sequence Score* AA Separation** Accession
Number(s)
Number of
residues
α-helical content, %*** β-strand content, %*** Purity****, % Mw, g/mol pI***** Net charge*****
(pH 7)
α-10 KKPVSKDSPETYEEALKRFAKLLSDRKKL 2.176 P15477 P11768 Q42502 Q3YJT3 29 26 7 92.7 3405.9 10.38 4
α-11 EALKRFAKLLSD 3.522 P15478 P15477 Q3YJT5 P11768 Q2MY60 Q2MY43 Q42502 Q3YJT3 12 97.0 1390.6 9.92 1
α-12 DSPETYEEALKRFAKLLSD 3.037 P15477 P11768 Q42502 Q3YJT3 19 74 5 94.9 2212.4 4.16 −2
α-13 NRPFAAAKDIVPFYFEHGPHIFN 2.155 P15477 P11768 Q42502 Q3YJT3 23 95.1 2688.0 7.53 0.2
α-14 AKDIVPFYFEHGPHIFN 2.255 P15477 P11768 Q42502 Q3YJT3 17 89.5 2031.3 6.05 -0.8
α-15 IPATILEFLEGQLQEVDNN 2.000 P15477 P11768 Q42502 Q3YJT3 19 86.3 2143.4 0.61 −4
α-16 ILEFLEGQLQEVDN 2.978 P15478 P15477 P11768 Q42502 Q3YJS9 Q3YJT3 14 83.7 1646.8 0.61 −4
α-17 KYDGKYLMQVLQE 2.029 P15478 Q3YJT5 Q2MY60 Q2MY43 Q3YJS9 13 89.8 1614.9 6.67 0
α-18 KYLMQVLQEKLGE 2.022 P15478 Q3YJT5 Q2MY60 Q3YJS9 13 96.8 1578.9 6.77 0
α-19 KYLMQVLQEKL 2.058 P15478 Q3YJT5 Q2MY60 Q3YJS9 11 74.5 1392.7 9.49 1
β-20 ELDSRLSYRIISTFWGALGGDVYLGKSPN 2.630 Q3S474 A0A097H149 Q66LL8 Q66LL2 29 75.0 3215.6 6.87 0
β-21 ELDSRLSYRIISTFWGALGGDVYL 3.131 Q3S474 A0A097H149 Q66LL8 Q66LL2 24 70.0 2732.0 4.17 −1
β-22 CPFSSDDQFCLKVGV 2.501 Q3S474 A0A097H149 L0AQL9 Q2XPX8 Q2XPY0 15 13 33 78.9 1644.9 3.71 −1.1
β-23 FIPLSTNIFEDQLLNIQFNIPT 2.391 Q3S488 Q3S482 Q3S479 H9B8I8 22 89.9 2577.9 0.69 −2
β-24 LNIQFNI 4.066 Q8RXA3 Q3S489 Q3S488 Q3S481 Q38M77 Q3S482 Q3S479 H9B8J1 H9B8I9 H9B8I8 H9B8J0 7 95.3 861 3.66 0
β-26 GKELDPRLSYRI 2.218 Q3S477 Q2XPX8 Q2XPY0 Q8LJQ0 12 86.9 1446.7 9.73 1
β-27 LNIQFNIPTPKLC 2.213 Q3S488 Q8RXA3 Q3S482 Q3S479 H9B8J1 13 23 31 70.6 1500.8 8.84 0.9
β-28 VHQNGKRRLALVKDNPLDVSFK 2.056 Q3S474 A0A097H149 Q2XPX8 Q2XPY0 22 94.2 2534.9 10.92 3.1
β-29 IGSSSHFGPHIFEGELLNIQFDIS 2.027 Q3S477 Q2XPX8 Q2XPY0 Q8LJQ0 24 84.7 2644.9 4.3 −2.8
β-30 DDNFCAKVGVVIQ 2.016 Q3S489 Q3S488 Q3S481 Q38M77 Q3S479 H9B8I9 13 80.3 1407.6 3.71 −1.1
β-31 LGGDVYLGKSPNSDAPCP 2.011 Q8RXA3 Q3S488 Q3S481 Q38M77 Q3S482 Q3S479 H9B8I9 H9B8I8 H9B8J0 18 91.8 1789.9 3.71 −1.1
γ-1 GIKGIIPAIILEFLEGQLQEVDNNKDAR 4.146 14 P15477 P11768 28 75 0 99.4 3094.5 4.2 −2
γ-34 CRDDNFCAKVGVVI 3.387 5 Q3S488 Q3S481 Q38M77 Q3S489 Q3S479 H9B8I9 14 89.0 1538.8 5.9 −0.1
γ-35 RDDNFCAKVGVVI 3.933 4 Q3S488 Q3S481 Q38M77 Q3S489 Q3S479 H9B8I9 13 87.8 1435.7 6.05 −0.1
γ-36 FDVIGGTSTGGLLTAMITTPNENNRP 3.190 17 P15477 Q3YJT5 P11768 Q2MY60 Q42502 Q3YJT3 26 31 23 78.6 2676.9 3.93 −1
γ-37 LLTAMITTPNENNRP 4.037 6 P15477 Q3YJT5 P11768 Q2MY60 Q42502 Q3YJS9 Q3YJT3 15 77.6 1684.9 6.86 0
γ−38 FCLKVGVVHQNGKRRLALVKDNP 3.168 8 Q3S474 Q2XPX8 A0A097H149 Q2XPY0 23 0 65 89.7 2592.1 10.91 4
γ-39 HQNGKRRLALV 4.790 7 Q3S474 Q3S477 Q2XPX8 A0A097H149 Q2XPY0 Q66LL8 Q66LL2 Q8LJQ0 11 98.3 1291.5 12.13 3.1
γ-40 SSDDQFCLKVGVV 3.137 5 Q3S474 Q2XPX8 A0A097H149 Q2XPY0 L0AQL9 13 0 46 80.6 1396.6 3.71 −1.1
γ-41 KDNPETYEEALKRFAKLLS 3.066 13 P15478 Q3YJT5 Q2MY60 Q2MY43 19 70.5 2252.5 6.88 0
γ-42 DTNGKELNPNSSYRIISIGRGALGGDVYL 3.055 14 Q3S481 Q38M77 Q3S489 H9B8I8 H9B8J0 29 79.0 3080.4 6.89 0
γ-43 NPNSSYRIISI 3.401 7 Q3S481 Q38M77 Q3S489 H9B8I8 H9B8J0 11 98.6 1263.4 9.41 1
γ-44 DNFCAKVGVVIQNGKRR 3.044 11 Q3S488 Q3S481 Q3S489 Q3S479 H9B8I9 17 72.3 1904.2 10.68 2.9
γ-45 VGVVIQNGKRR 4.779 5 Q8RXA3 Q3S488 Q3S481 Q3S489 Q3S482 Q3S479 H9B8J1 H9B8I9 H9B8J0 11 94.6 1225.5 12.13 3
γ-46 FAKLLSDRKKLRANK 3.043 5 P15478 P15477 P11768 Q2MY60 Q2MY43 Q42502 Q3YJS9 Q3YJT3 15 95.2 1788.2 11.57 5
γ-47 TPNENNRPFAAAKDIV 3.024 8 P15477 Q3YJT5 P11768 Q42502 Q3YJT3 16 97.3 1756.9 6.62 0
γ-48 GIIPATILEFLEGQLQEVDNN 3.003 11 P15478 Q42502 Q3YJS9 Q3YJT3 21 92.2 2313.6 0.61 −4
γ-49 FCLKVGVIHQNGKRRLALVK 2.478 8 Q3S477 Q8LJQ0 20 0 75 99.0 2279.8 11.49 5

*Predicted amphiphilic score.

**AA used by the algorithm to define the divide between the hydrophobic and hydrophilic part of the peptide.

***Fraction of residues located in a given secondary structure conformation (within the native protein) as implied by homology modelling. This was carried out only for the 9 selected peptides.

****Purity of the synthetic peptides used as received from pepMic Co., Ltd (Jiangsu, China).

*****pI and net charge were calculated by using peptide property calculator from INNOVAGEN (Innovagen AB, Lund, Sweden).