Specific Interactions Between Sense and Complementary Peptides: The Basis for the Proteomic Code

Inhibition ofβ-Amyloid Aggregation and Neurotoxicity by Complementary (Antisense) Peptides

“…[11] Furthermore, peptides coded for by sense and complementary strands of DNA are actually able to interact specifically in a way that may be comparable to the specific interaction between the two strands of DNA. [12] By definition, a complementary peptide is coded for by the nucleotide sequence (read 5' 33') of the complementary strand of DNA (or, more precisely, by codons in complementary mRNA whose sequence contains the same coding information as the complementary strand of DNA). The codons in complementary mRNA may also be read continuously in the 3' 35' (Root ± Bernstein direction) to give an alternative complementary peptide (Table 1).…”

“…The codons in complementary mRNA may also be read continuously in the 3' 35' (Root ± Bernstein direction) to give an alternative complementary peptide (Table 1). [12,13] Our approach to devising a novel inhibitor of Ab fibrilisation has been to exploit this concept of complementary peptides, including importantly the concept of 3' 35' complementary peptides. The shortest region of Ab able to aggregate and display neurotoxic properties corresponds to the C-terminal amino acid residues.…”

Role of complementary proteins in autoimmunity: an old idea re-emerges with new twists

“…Three main theories, proposed by Root-Bernstein and Holsworth [10], Siemion et al [11] and Smith et al [6], have been put forward to explain this proposed symmetry [5,[10][11][12][13][14][15][16]. All three hypotheses use ideas regarding amino acid interactions developed by Meckler [17] and all three have been exploited to design complementary peptides that can be used to block protein-ligand interactions [15,[18][19][20][21] or to design vaccines [5,9].…”

Study on peptide-peptide interaction using high-performance affinity chromatography and quartz crystal microbalance biosensor

“…As predicted by Mekler [1] and first shown experimentally by Bost et al [2] , an antisense peptide could interact with the corresponding sense peptide at some degree of selectivity. The interaction between sense and antisense peptides has been reported [3,4] . As such interaction is specific and selective, its application in affinity technology has been widely achieved.…”

“…Two main hypotheses have been put forward to explain the specific interactions between sense peptide and antisense peptide. As defined by Heal et al in 2002 [4] , one is called Mekler-Idlis (M-I) pair theory while the other is called molecular recognition theory (MRT). According to M-I pair theory, each codon-directed amino acid residue in a given sense peptide can interact with its corresponding codon-directed amino acid residue in antisense peptide in a specific and pair-wise way.…”