The use of complementary peptides in the purification of an angiotensin II binding protein

Ts, Elton; Oparil, Suzanne; Je, Blalock

doi:10.1097/00004872-198812040-00127

Cited by 6 publications

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“…The results of direct binding studies between 125I-IGF-I [21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36][37][38][39][40] and I-FGI 20-40 are shown in Table 2. In these experiments I-FGI 20-40, control peptides 1 and 2 and BSA (10 ,tg of each) were absorbed into wells of microtitre plates, and the binding of 125I-IGF-I 21-40 was examined.…”

Section: Resultsmentioning

confidence: 99%

“…Nevertheless, despite this body of supportive evidence, the area remains controversial in that some reports have questioned the universality of the theory. For example, two recent studies have found no evidence for interaction between the octapeptide angiotensin II and the corresponding complementary peptide [18,19], thus contradicting earlier observations with these two peptides [20,21]. Similarly no evidence of binding between human parathyroid hormone fragment (hPTH 1-40) and its corresponding complementary peptide was obtained [22].…”

Section: Introductionmentioning

confidence: 86%

“…Because of these conflicting data, and owing to the potential significance of the molecular-recognition theory in the areas of drug design, evolution of polypeptide ligand-receptor genes and idiotypic/anti-idiotypic antibody networks [12,28], we have reexamined this theory using human-insulin-like-growth-factor-I fragment [21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36][37][38][39][40] and its complementary peptide (I-FGI 20-40). We report data on the binding of this peptide pair in solid-and solution-phase assays and of the behaviour of I-FGI 20-40 in radioimmuno-(r.i.a.)…”

Section: Introductionmentioning

confidence: 99%

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Critical evaluation of a theory of molecular recognition using human insulin-like-growth-factor-I fragment 21–40 and its complementary peptide

Beattie

Flint

1992

Biochemical Journal

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Using solid-phase methods we have synthesized human insulin-like-growth-factor-I (IGF-I) fragment 21-40 (IGF-I 21-40) and the peptide derived from the 5'----3' translation of the complementary nucleic acid of this peptide, 'I-FGI 20-40' (the complementary peptide). According to a recently proposed theory of molecular recognition, these two peptides should bind specifically to each other. We have tested this theory by using both solid- and solution-phase direct-binding assays for this complementary-peptide pair. We have also investigated the ability of I-FGI 20-40 to interfere with native IGF-I binding during radioimmunoassay (r.i.a.), radio-receptor (r.r.a.) assay and ligand-blot analysis of IGF-binding proteins. We have obtained no evidence of any interaction between IGF-I 21-40 and I-FGI 20-40 in either solid- or solution-phase assays. In addition, I-FGI 20-40 does not interfere in the assays used to detect IGF-I binding antibodies (r.i.a.), receptors (r.r.a.) or binding proteins (ligand blots). Our data therefore question the universality of this particular theory of molecular recognition.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 86%

Section: Introductionmentioning

confidence: 99%

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Critical evaluation of a theory of molecular recognition using human insulin-like-growth-factor-I fragment 21–40 and its complementary peptide

Beattie

Flint

1992

Biochemical Journal

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“…Indeed, since the early studies by Blalock and coll. (23,26), there have been several systems in which complementary peptides have been produced and employed; fibrinogen, laminin receptor, angiotensin II, arginine vasopressin, beta-endorphin, growth hormone releasing peptide, and acetyl choline receptor, among others (28)(29)(30)(31)(32)(33)(34)(35). In 2002, Goicoechea et al (36) utilized the concept of inverse hydropathy to demonstrate that the interaction between thrombospondin and cell surface calreticulin was due to opposite hydropathic profiles between multiple peptide sequences in the proteins.…”

Section: Molecular Recognition Theory and Sense/anti-sense Interactionmentioning

confidence: 99%

Molecular recognition theory and sense-antisense interaction therapeutic applications in autoimmunity

Blalock¹

2012

Front Biosci

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Perhaps behind only the understanding of the genetic code in importance is the comprehension of protein sequence and structure in its effect on modern scientific investigation. How proteins are structured and interact dictates a considerable amount of the body's processes in maintaining homeostasis. Unfortunately, in diseases of autoimmunity, these processes are directed against the body itself and most of the current clinical responses are severely lacking. This review addresses current therapeutics involved in the treatment of various autoimmune diseases and details potential future therapeutics designed with a more targeted approach. Detailed in this manuscript is the concept of utilizing peptides possessing an inverse hydropathy to the immunogenic region of proteins to generate anti-idiotypic (anti-Id) and anti-clonotypic T cell receptor (TCR) antibodies (Abs). Theoretically, the anti-Id Abs cross react with Id Abs and negate the powerful machinery of the adaptive immune response with little to no side effects. A series of studies by a number of groups have shown this to be an exciting and intriguing concept that will likely play a role in the future treatment of autoimmune diseases.

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“…Finally, investigators have synthesized antisense peptide sequences based on two different reading frames of Ang II mRNA (parallel and antiparallel; see later section) resulting in Ang II antagonist activity. [5][6][7][8][9][10][11][12][13] This study focuses on Ang II antisense peptide activity. 14,15 Two fundamentally different approaches to antisense peptide design have been used to generate both Ang II antipeptides and antisense peptides against other peptide targets.…”

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confidence: 99%

Augmentation of Aortic Ring Contractions by Angiotensin II Antisense Peptide

1998

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Abstract-Previous biochemical experiments have revealed two antisense peptide antagonists to human angiotensin II (Ang II), one encoded in the cDNA in the antiparallel reading, the other in the parallel reading. Neither peptide's ability to produce physiological antagonism has been demonstrated previously. Both peptides were tested for their ability to antagonize Ang II-induced contractions on rabbit aorta smooth muscle. Neither peptide had any direct contractile activity. The antiparallel Ang II peptide had physiological antagonism to Ang II contractions at a lower sensitivity than reported in biochemical studies, and its antagonist activity was partially blocked by Ang II antiserum, suggesting that it is not an antipeptide but an Ang II homologue. The parallel Ang II antipeptide also required high concentrations for physiological inhibition. Its contractile inhibition was not affected by Ang II antiserum and diminished the Ang II contraction at high micromolar concentrations, findings consistent with physicochemical data showing that it is an Ang II complement. The concentration of either peptide required to produce an antagonistic physiological effect was too high to predict any pharmacological usefulness. The parallel antipeptide, however, significantly increased the force of muscle contractions at high nanomolar concentrations, thus displaying a unique dual augmentation/antagonist activity. This antipeptide seems to have highly sequence-specific activity because other similar parallel antipeptides had no activity. The parallel antipeptide augmentation mimics the shift in the Ang II dose-response curve produced in hypertension studies of the slow pressor effect of Ang II and may be useful in deducing the currently unknown cause of the slow pressor effect. It may also have some uses in migraine studies. (Hypertension. 1998;31:854-860.)

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The use of complementary peptides in the purification of an angiotensin II binding protein

Cited by 6 publications

References 0 publications

Critical evaluation of a theory of molecular recognition using human insulin-like-growth-factor-I fragment 21–40 and its complementary peptide

Critical evaluation of a theory of molecular recognition using human insulin-like-growth-factor-I fragment 21–40 and its complementary peptide

Molecular recognition theory and sense-antisense interaction therapeutic applications in autoimmunity

Augmentation of Aortic Ring Contractions by Angiotensin II Antisense Peptide

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