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. Author manuscript; available in PMC: 2008 Aug 17.
Published in final edited form as: Biochemistry. 2006 Jun 20;45(24):7586–7597. doi: 10.1021/bi0603928

Table 2.

Peptides used in this study

Name Sequence a % Response (n)b
Peptide 1c EMPGVLRF-NH2 100
Peptide 2d graphic file with name nihms61165t1.jpg 29.1±5.7 (16)
Peptide 3 graphic file with name nihms61165t2.jpg 0 (3)
Peptide 4 graphic file with name nihms61165t3.jpg 19.0±2.6 (8)
Peptide 5 SGSGAMPGVLRF-NH2 118.7±11.0 (4)
Peptide 6 AAAAAMPGVLRF-NH2 62.4±3.2 (10)
Peptide 7e graphic file with name nihms61165t4.jpg 49.3±16.5 (4)
Peptide 8 graphic file with name nihms61165t5.jpg 0 (3)
Peptide 9f graphic file with name nihms61165t6.jpg 45.0±10.5 (6)
Peptide 10g graphic file with name nihms61165t7.jpg 104.8±2.8 (8)
Peptide 11 PGVLRF-NH2 43.0±5.5 (14)
Peptide 12 PGVLRFPGVLRF-NH2 198.1±33.3 (10)
a

Naturally occurring sequences are underlined. The conserved PGVLRF-NH2 sequence is in bold. N-terminal “extension” sequences of native long flp-18 peptides are bold and: Red for C. elegans based sequences and Blue for A. suum based sequences.

b

Peptides (10-6 M) were applied in 2 m pulses to Xenopus oocytes expressing NPR-1 215V. Results expressed as a % of response to 10-6 M Peptide 1 (EMPGVLRF-NH2) +/- SEM

c

Most active native C. elegans FLP-18 peptide

d

Longest and least active native FLP-18 peptide

e

Longest Ascaris AFP-1 peptide

f

Chimera of long FLP-18 + long AFP-1

g

Chimera of long AFP-1 + long FLP-1