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. Author manuscript; available in PMC: 2008 Apr 1.
Published in final edited form as: Peptides. 2007 Jan 4;28(4):887–892. doi: 10.1016/j.peptides.2006.12.002

Table 1.

TIP39 analogs screeneda

−1 1 2 3 4 5 6 7 8 9 10 11 12 % Maximal PTH2-R activationb
S L A L A D D A A F R E 1E-06 1E-07 1E-08
A 100 100 79
A 100 100 100
A 100 85 0
A 100 100 100
A 100 100 100
E 100 100 100
F 100 100 100
H 100 100 100
I 100 100 100
V 100 100 100
W 100 100 100
Y 100 100 100
V 87 77 62
W 69 63 45
P 72 67 18
L 41 52 51
H 56 59 52
F 60 46 41
S 50 61 55
L 3 0 0
K 50 0 0
S 54 1 0
V 5 0 0
E 82 65 71
Q 65 26 0
R 0 0 0
A 100 0 0
W 0 0 0
M 73 0 0
T 23 0 0
H 23 6 1
W H 0 1 0
Y W H 0 1 0
P Y W H 1 1 1
H Y W H 0 0 0
H Y W G 5 4 3
H Y W D 10 6 9
H Y W A 0 3 5
H Y W V 9 7 5
H Y W I 4 3 5
H Y W T 9 7 9
H Y W N 6 7 9
a

The first 12 amino acid residues of TIP39 are indicated at the top. The analogs screened are indicated on subsequent rows. Either a single addition or substitution, or several substitutions, were incorporated as indicated. Standard single letter amino acid code.

b

The percentage of the amount of cAMP accumulation produced by 1nM unmodified TIP39, in the presence of 10−6, 10−7 or 10−8 mutant peptide, in single screening experiments.