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Table 3 The influence of single point Tat amino acid substitutions on Tat-TAR binding affinity

From: HIV-1 Tat amino acid residues that influence Tat-TAR binding affinity: a scoping review

Tat amino acid position

Mutation

Binding affinity

Percentage increase/decrease in Tat-TAR binding affinity

Technique

References

5

R5K

6.7 × 10−7 M

70% decrease

Surface plasmon resonance (SPR)

[86]

49

K49A

4 × 10−6 M

1900% decrease

Absorption spectroscopy, Gel shift assays, CD Spectroscopy

[71]

50

K50A

2 × 10–5 M

9900% decrease

Absorption spectroscopy, Gel shift assays, CD Spectroscopy

[71]

51

K51A

4 × 10−6 M

1900% decrease

Absorption spectroscopy, Gel shift assays, CD Spectroscopy

[71]

52

R52A

10 × 10−9 M

40% decrease

Electrophoretic mobility shift assay (EMSA)

[69]

53

R53A

12 X 10−9 M

50% decrease

EMSA

[69]

K53A

4 × 10−6 M

1900% decrease

Absorption spectroscopy, Gel shift assays, CD Spectroscopy

[71]

54

Q54A

5 X 10−9 M

20% increase

EMSA

[69]

8 × 10−8 M

12.5% decrease

Fluorescence resonance energy transfer (FRET), MALDI-TOFMS, Fluorescence binding assay

[82]

K54A

2 × 10–5

1900% decrease

Absorption spectroscopy, Gel shift assays, CD Spectroscopy

[71]

55

R55A

12 × 10−9 M

50% decrease

EMSA

[69]

56

R56A

12 × 10−9 M

50% decrease

EMSA

[69]

K56A

4 × 10−6 M

1900% decrease

Absorption spectroscopy, Gel shift assays, CD Spectroscopy

[71]