Skip to main content

Table 3 Amylin Mutations generated by FibrilMutant with destabilizing potential

From: Computational re-engineering of Amylin sequence with reduced amyloidogenic potential

Original

Residue no.

Mutated

Disruption

TANGO

amino acid

 

amino acid

method

rank

A

13

R

Making core charged

1

F

15

P

Mutating an amino acid on a beta strand

2

F

15

D

Making core charged

3

L

16

D

Making core charged

4

A

25

R

Making core charged

5

I

26

R

Making core charged

6

G

24

P

Mutating GLY at a turn

7

L

27

R

Making an amino acid on a beta strand charged

8

F

23

E

Making core charged

9

G

24

D

Making core charged

10

V

17

E

Making core charged

11

Q

10

H

Making protein surface hydrophobic

12

N

21

P

Mutating an amino acid at a turn

14

C

2

Q

Making protein surface hydrophobic

15

T

6

M

Making protein surface hydrophobic

16

T

4

S

Making protein surface hydrophobic

17

V

32

K

Making an amino acid on a beta strand charged

18

N

3

H

Making protein surface hydrophobic

19

A

8

E

Making an amino acid on a beta strand charged

20

T

9

N

Making protein surface hydrophobic

21

L

12

E

making core charged

23

C

7

T

Making protein surface hydrophobic

24

G

33

E

Making an amino acid on a beta strand charged

25

S

20

G

Discovered experimentally [29]

13

S

20

K

Discovered experimentally [29]

22

N

21

L

Discovered experimentally [56]

26

N

14

L

Discovered experimentally [56]

27

  1. Mutations above the horizontal line are destabilizing mutations proposed by FibrilMutant, and mutations below the line have been suggested and tested experimentally. Mutations are ranked by TANGO from lowest aggregation potential to highest aggregation potential.